CYTOSKELETON Flashcards

1
Q

families of protein filaments

A

actin filaments, microtubules, intermediate filaments

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2
Q

shape of the cell’s surface; whole-cell locomotion; pinching of one cell into two

A

actin filaments

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3
Q

positions of membrane-enclosed organelles; direct intracellular transport; from the mitotic spindle during cell division

A

microtubules

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4
Q

mechanical strength; protective cage for the cell’s DNA; form tough appendages (hair and fingernails)

A

intermediate filaments

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5
Q

cell-surface projections class of actin filaments

A

lamellipodia and filopodia

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6
Q

motile whips or sensory devices of cells

A

cilia

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7
Q

belt around the middle of the cell; pinches the cell into two identical sister cells

A

contractile ring

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8
Q

protrusive structure filled with newly polymerized actin filaments

A

neutrophils

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9
Q

specialized epithelial cells in the intestines and lungs

A

microvilli and cilia

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10
Q

present in the apical surface and the basolateral surface; maintain strong adhesive contacts with one another to enable this single layer of cells to serve as an effective physical barrier

A

polarized epithelial cells

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11
Q

actin filaments are made of ________ using ATP hydrolysis

A

actin subunits

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12
Q

microtubules are made from clusters of _________ through __________ hydrolysis

A

tubulin subunits, GTP

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13
Q

polarized structural proteins; asymmetrical form; polarized

A

actin filaments and microtubules subunits

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14
Q

determine the spatial distribution and the dynamic behavior of the filaments; bind to the filaments or their subunits to determine the sites of assembly of new filaments

A

accessory proteins

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15
Q

bind to a polarized cytoskeletal filament; energy from ATP hydrolysis to move along the filament, and the “cargo” they carry

A

motor proteins

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16
Q

tubulin homolog; generate a bending force that drives the membrane invagination and site for localization of enzymes

A

FtsZ

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17
Q

actin homolog; scaffold to direct the synthesis of the peptidoglycan cell wall

A

MreB and Mbl

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18
Q

abnormalities in cell shape and defects in chromosomes segregation

A

mutations

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19
Q

bacterial actin homolog; encoded by a gene on certain bacterial plasmids that also carry genes responsible for antibiotic resistance

A

ParM

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20
Q

homolog of intermediate filaments

A

Caulobacter crescentus – crescentin

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21
Q

structural proteins present in muscle cells

A

α-Actin

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22
Q

almost non-muscle cells

A

β- and γ-actins

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23
Q

faster-growing; barbed end

A

plus end

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24
Q

pointed end; slower-growing

A

minus end

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25
Q

the minimum length at which random thermal fluctuations are likely to cause it to bend

A

persistence length

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26
Q

assembly of actin subunits

A

head-to-tail → tight, subunits right-handed helix

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27
Q

assemble into an initial aggregate, or nucleus, that is stabilized by multiple subunit–subunit contacts and can then elongate rapidly by addition of more subunits

A

nucleation

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28
Q

G-actin proceeds in three sequential phases:

A

nucleation, elongation, steady-state

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29
Q

rapidly increases in length by the addition of actin monomers to both of its ends

A

elongation

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30
Q

G-actin monomers exchange with subunits at the filament ends, but there is no net change in the total mass of filaments

A

steady-state

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31
Q

when steady-state phase has been reached, the concentration of the pool of unassembled subunits is called

A

critical concentration, Cc

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32
Q

the ratio of the “on” and “off” rate constant; measures the concentration of G-actin where the addition of subunits is balanced by the dissociation of subunits

A

dissociation constant

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33
Q

manifested by the different rates at which G-actin adds to the two ends

A

polarity of F-actin

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34
Q

difference in elongation rates at the opposite ends of an actin filament is caused by a ______________________at the two ends

A

difference in Cc values

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35
Q

actin can only elongate in the _________

A

minus end

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36
Q

actin can only elongate in the __________ when the minus end is blocked

A

plus end

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37
Q

G-actin concentration below Cc+, there is:

A

no filament growth

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38
Q

G-actin concentrations between Cc+ and Cc-

A

growth is only at the (+) end

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39
Q

G-actin concentration above

A

no growth at both ends

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40
Q

G-actin concentrations intermediate between the Cc values for the (+) and the (-) ends, subunits continue to be added at the (+) end and lost from the (-) end

A

steady-state phase

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41
Q

newly added subunits traveling through the filament, as if on a

A

treadmill

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42
Q

actin behavior is regulated by _____________ that bind actin monomers or filaments

A

accessory proteins

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43
Q

a measure of how long an individual actin monomer spends in a filament as it treadmills

A

filament half-life

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44
Q

inhibition of actin polymerization; they cannot associated with either the plus or minus ends; neither hydrolyze nor exchange their bound nucleotide

A

thymosin

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45
Q

binds to the face of the actin monomer opposite the ATP-binding cleft, blocking the side of the monomer that would normally associate with the filament minus end, while leaving exposed the site on the monomer that binds to the plus end

A

profilin

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46
Q

prerequisite for cellular actin polymerization

A

filament nucleation

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47
Q

actin-related proteins; nucleates actin filament growth from the minus end, allowing rapid elongation at the plus end

A

Arp 2/3 complex

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48
Q

dimeric proteins that nucleate the growth of straight, unbranched filaments that can be cross-linked by other proteins to form parallel bundles

A

formins

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49
Q

Formin-dependent actin filament growth is strongly enhanced by the association of actin monomers with

A

profilin

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50
Q

side-binding proteins; elongated protein that binds simultaneously to six or seven adjacent actin subunits

A

tropomyosin

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51
Q

binds at the plus end; stabilizes an actin filament (inactive)

A

capping protein (CapZ)

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52
Q

capping long-lived actin filaments in muscle; minus end-binding; binds tightly to the minus ends that have been coated and stabilized by tropomyosin

A

tropomodulin

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53
Q

coats the filament completely and present in high amounts

A

side-binding

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54
Q

affect filament dynamics

A

end-binding

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55
Q

proteins that break an actin filament into many smaller filaments; generating new filament ends

A

severing proteins

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56
Q

activated by high levels of cytosolic Ca2+; interacts with the side of the actin filament and contains subdomains that bind to two different sites

A

gelsolin superfamily

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57
Q

actin depolymerizing factor; binds along the length of the actin filament, forcing the filament to twist a little more tightly

A

cofilin

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58
Q

actin filament types of arrays

A

dendritic networks, bundles networks, weblike (gel-like) networks

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59
Q

made of the long, straight filaments produced by formins

A

bundles networks

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60
Q

Arp 2/3 complex

A

dendritic networks

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61
Q

diff. actin networks depends on:

A

specialized accessory proteins

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62
Q

cross-link actin filaments into parallel array

A

bundling proteins

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63
Q

hold two actin filaments together at a large angle to each other, forming a looser meshwork

A

gel-forming proteins

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64
Q

enable stress fiber and other contractile arrays to contract

A

myosin II

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65
Q

close packing of actin filaments; not contractile

A

fimbrin

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66
Q

cross-links oppositely polarized actin filaments into loose bundle; allowing the binding of myosin and formation of contractile actin bundles

A

α-actinin

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67
Q

formation of a loose and highly viscous gel; by clamping together two actin filaments roughly at right angles; form actin filament webs or gels

A

filamin

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68
Q

cytoskeletal protein actin projection on the leading edge of the cell; determines cell movement direction by protrusive force that arises from the actin network

A

lamellipodia

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69
Q

defect in nerve-cell migration during early embryonic development

A

filamin A gene mutations

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70
Q

periventricular region of the brain fail to migrate to the cortex and instead form nodules

A

periventricular heterotopia

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71
Q

web-forming; long, flexible protein made out of four elongated polypeptide chains; allows RBC to “spring back” to shape

A

spectrin

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72
Q

first motor protein identified; generates force for muscle contraction

A

myosin

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73
Q

an elongated protein formed from two heavy chains and two copies of each light chains

A

myosin II

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74
Q

globular head domain at its N-terminus; contains force-generating machine

A

heavy chain

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75
Q

bind close to the N-terminal head of myosin

A

light chains

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76
Q

MYOSIN: SLIDING FILAMENT THEORY

A
  • myosin head binds and hydrolyzes ATP
  • it then uses the energy from ATP hydrolysis to walk toward the plus end of an actin filament
    [opposing orientation of the heads makes the filament efficient at sliding]
  • ATP-driven sliding of actin filaments results in a powerful contraction
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77
Q

each step of the movement along actin is generated by the swinging of an:

A

8.5nm long α-helix – lever arm

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78
Q

a piston-like helix that connects movements at the ATP-binding cleft in the head to small rotations

A

converter domain

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79
Q

changes in the conformation of the myosin are coupled to changes in its:

A

binding affinity for actin

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80
Q

a cylindrical structure 1-2 μm in diameter that is often as long as the muscle cell itself

A

myofibril

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81
Q

myofibrils is made up of a long, repeated chain of tiny contractile units called _________, which gives the vertebrate myofibril its striated appearance

A

sarcomeres

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82
Q

parallel and partly overlapping thin and thick filaments

A

sarcomeres

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83
Q

myosin filaments sliding past the actin thin filaments, with no change in the
length of either type of filament causes:

A

sarcomere shortening

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84
Q

initiates muscle contraction; signal passes to the skeletal muscle from the nerve that stimulates it

A

rise in cytosolic Ca2+

85
Q

two major features of the muscle cell make extremely rapid contraction possible

A
  1. myosin motor heads coupled binding and hydrolysis to ATP
  2. a specialized membrane system relays the incoming signal rapidly throughout the entire cell
86
Q

MUSCLE MOVEMENT: Ca+ Signaling

A
  • signal from the nerves triggers an action potential that signals the T tubules (transverse tubules)
  • T tubules conducts the action potential to the sarcoplasmic reticulum which triggers the release of Ca2+ channels in the sarcoplasmic reticulum
  • Ca2+ flooding into the cytosol then initiates the contraction
87
Q

elongated protein that binds along the groove of the actin filament helix

A

tropomyosin

88
Q

complex of three polypeptides (T, I, & C)

A

troponin

89
Q

elevated intracellular Ca2+ levels regulate contraction by a mechanism that depends on:

A

calmodulin

90
Q

induces the phosphorylation of smooth muscle myosin on one of its two light chains; activated by Ca2+-bound calmodulin

A

myosin light-chain kinase (MLCK)

91
Q

common cause of sudden death in young athletes; heart enlargement, abnormally small coronary vessels, disturbances in heart rhythm

A

familial hypertrophic cardiomyopathy

92
Q

minor missense mutations in the cardiac actin gene

A

dilated cardiomyopathy

93
Q

distinct myosin families

A

37

94
Q

human genome includes ___ myosin genes

A

40

95
Q

intracellular organization; microvilli and endocytosis

A

myosin I

96
Q

two-headed myosin with a large step size; organelle transport along actin filaments; move progressively along actin filaments without letting go

A

myosin V

97
Q

actin cables in the mother cell point toward the bud, where actin is found in patches that concentrate where cell wall growth is taking place

A

Saccharomyces cerevisiae

98
Q

highly dynamic and play comparably diverse and important roles in the cell; polymers of tubulin

A

MICROTUBULES

99
Q

longitudinal axis - “top” of β-tubulin molecule forms an interface with the “bottom” of the α-tubulin molecule in the adjacent heterodimer; lateral
contacts, α–α and β–β

A

protein-protein contact

100
Q

microtubules dynamics is influenced by the:

A

hydrolysis of GTP

101
Q

GTP hydrolysis occurs only within

A

β-tubulin

102
Q

bound GTP

A

T form

103
Q

bound GDP

A

D form

104
Q

GTP tubulin tends to ________, and GDP-tubulin to ____________

A

polymerize, depolymerize

105
Q

high rate of addition – the tip of the polymer remains in the T form

A

GTP cap

106
Q

rapid interconversion between a growing and shrinking state

A

dynamic instability

107
Q

growth to shrinkage

A

catastrophe

108
Q

shrinkage to growth

A

rescue

109
Q

tubulins subunits with GTP bound to the β-monomer produce __________ that make strong and regular lateral contacts with one another

A

straight protofilaments

110
Q

associated with subtle conformational change in the protein - curved

A

hydrolysis of GTP to GDP

111
Q

constrain the curvature of the protofilaments, the ends appear straight; terminal subunits have hydrolyzed, constrains is removed, spring apart

A

GTP cap

112
Q

microtubules functions are inhibited by both:

A

polymer-stabilizing and polymer destabilizing drugs

113
Q

causes microtubule depolymerization

A

colchicine and nocodazole

114
Q

binds to and stabilized microtubules; increase in tubulin polymerization; used to treat cancers of the breast and lung

A

taxol

115
Q

microtubule-depolymerizing and polymerizing drugs preferentially

A

kill dividing cells

116
Q

smaller amounts, involved in the nucleation of microtubule growth

A

γ-tubulin

117
Q

where specific intracellular location microtubules nucleation occurs

A

microtubule-organizing center (MTOC)

118
Q

two accessory proteins bind directly to the γtubulin, along with several other proteins that help create a spiral ring of γ-tubulin molecules, which serves as a template that creates a microtubule with 13 protofilaments

A

γ-tubulin ring complex (γ-TuRC)

119
Q

well-defined MTOC; located near the nucleus

A

centrosome

120
Q

embedded in the centrosome; a pair of cylindrical structures arranged at right angles in an L-shaped configuration; barrel shape with striking nine-fold symmetry

A

centrioles

121
Q

where microtubule nucleation takes place

A

pericentriolar material

122
Q

MTOC embedded in the nuclear envelope found in budding yeast, fungi, and diatoms; no centrioles in fungi or plants; use γ-tubulin to nucleate their
microtubules

A

spindle pole body

123
Q

dynamic plus ends pointing outward toward the cell periphery and stable minus ends collected near the nucleus

A

aster-like configuration

124
Q

proteins that bind to microtubules; stabilize against disassembly; mediate interactions with other cell components – prominent in neurons, axons and dendrites that extend from the cell body

A

microtubule-associated proteins (MAPs)

125
Q

long projecting domain; form bundles of stable microtubules that are widely spaced

A

MAP2

126
Q

shorter projecting domain, form bundles of more closely packed microtubules

A

tau

127
Q

bind to microtubule ends and appear to pry protofilaments apart

A

catastrophe factors (kinesin-13)

128
Q

protects microtubule minus ends from the effects of catastrophe factors

A

Nezha / Patronin

129
Q

enriched at microtubule plus ends; binds free tubulin subunits and delivers them to the plus end; promoting microtubule polymerization and simultaneously counteracting catastrophe factor activity

A

XMAP215

130
Q

stabilized by association with a capping protein or the centrosome; depolymerization sites

A

minus ends

131
Q

explore and probe the entire cell space

A

plus ends

132
Q

accumulate at these active ends (+) and appear to rocket around the cells as passengers at the ends of rapidly growing microtubules; dissociating from the ends when microtubules shrink

A

plus-end tracking proteins (+TIPs)

133
Q

modulate the growth and shrinkage of microtubule; control microtubule positioning

A

kinesin-related catastrophe factors and XMAP215

134
Q

small dimeric proteins; attach to the plus end; allow the cell to harness the energy of polymerization; used for positioning the spindle, chromosomes, or organelles

A

EB1

135
Q

unpolymerized tubulin subunits to maintain a pool of active subunits

A

cell sequester

136
Q

binds to two tubulin heterodimers and prevents their addition to the ends of microtubules; decrease the effective concentration of tubulin subunits

A

stathmin (Op18)

137
Q

“sword”; made up for two subunits, smaller ones hydrolyze ATP performs the actual severing, larger on directs katanin to the centrosome

A

katanin

138
Q

two types of motor proteins:

A

kinesins and dyneins

139
Q

carriers membrane-enclosed organelles away from the cell body toward the axon terminal by walking toward the plus end of microtubule

A

kinesin-1 (“conventional kinesin”)

140
Q

distinct families in kinesin superfamily

A

14

141
Q

depolymerize microtubule ends

A

ATP hydrolysis

142
Q
A
143
Q

minus-end directed motors; one, two, or three heavy chains and large and variable number of associated intermediate, light-intermediate, and light
chains

A

dyneins

144
Q

homodimers of two heavy chains

A

cytoplasmic dyneins

145
Q

organelle and mRNA trafficking, for positioning the centrosome and nucleus during cell migration, construction of the microtubule spindle

A

cytoplasmic dynein I

146
Q

cilia, transport material from the tip to the base of the cilia

A

cytoplasmic dynein II

147
Q

highly specialized for the rapid and efficient sliding movements of microtubules that drive the beating of cilia and flagella; largest of the known molecular motors;
fastest

A

axonemal dyneins (ciliary dyneins)

148
Q

responsible for fast antegrade axonal transport → movements toward the cell’s periphery

A

kinesin

149
Q

retrograde axonal transport → movement towards the cell center

A

cytoplasmic dynein

150
Q

large protein complex associated to cytoplasmic dynein; to translocate organelles
effectively

A

dynactin

151
Q

cells fail to migrate to the cerebral cortex of the developing brain

A

smooth brain (lissencephaly)

152
Q

a dynein-binding protein, required for nuclear migration in several species

A

Lis1

153
Q

contain large pigment granules that can alter their location in response to neuronal or hormonal stimulation

A

fish melanocytes

154
Q

assembly depends on reorganization of the interphase array of microtubules to form bipolar array of microtubules

A

mitotic spindle

155
Q

receive signals; mixed polarities of microtubules

A

dendrites

156
Q

transmit signals; minus end pointing back toward the cell body, the plus end pointing toward the axon terminals

A

axons

157
Q

highly specialized and efficient motility structures built from microtubules and dynein

A

cilia and flagella

158
Q

found on sperm and many protozoa; undulating motion, they enable the cells to which they are attached to swim through liquid media

A

flagella

159
Q

cell organelle which beats with a whip-like motion that resembles the breaststroke in swimming

A

cilia

160
Q

cell movement is produced by the bending of its core, which is called the

A

axoneme

161
Q

form bridges between the neighboring doublet microtubules around the circumference of the axoneme

A

axonemal dynein

162
Q

hereditary defects in axonemal dynein causes -

A

ciliary dyskinesia or Kartagener’s syndrome

163
Q

bacterial flagella

A

flagellin

164
Q

nonmotile counterpart of cilia and flagella; specialized cellular compartments or organelles; shares structural features with motile cilia

A

primary cilium

165
Q

nine groups of fused fused triplet microtubules arranged in a cartwheel

A

centriole

166
Q

converting light to neural signal

A

rod and cone cells of retina

167
Q

odorant reception and signal amplification

A

nasal epithelium

168
Q

forms a cytoplasmic filament ; cells that are subject to mechanical stress

A

INTERMEDIATE FILAMENTS

169
Q

made up of an equal mixture of type I (acidic) and type II (neutral/basic) keratin proteins → heterodimer

A

keratin filament

170
Q

epithelial cancers

A

carcinomas

171
Q

cell-cell contact

A

desmosomes

172
Q

cell-matrix contact

A

hemidesmosomes

173
Q

defective keratins in the basal cell layer of the epidermis

A

epidermolysis bullosa complex

174
Q

intermediate filaments found in high concentrations along axons

A

neurofilaments

175
Q

influences how fast electrical signals travel down the axon; influenced by neurofilament gene expression

A

axonal diameter

176
Q

ALS, or Lou Gehrig’s disease

A

amyotrophic lateral sclerosis

177
Q

expressed in skeletal, cardiac, and smooth muscle, where it forms a scaffold around the Z disc of the sarcomere

A

Desmin

178
Q

stabilize microtubules against depolymerization

A

vimentin-like filaments

179
Q

scaffolds for proteins that control myriad cellular processes including transcription, chromatin organization, and signal transduction

A

A-type lamins

180
Q

associated with mutant versions of lamin A and include tissue-specific diseases

A

laminopathies

181
Q

The intermediate filament network is linked to the rest of the cytoskeleton by members of a family of proteins called

A

plakins

182
Q

large and modular, containing multiple domains that connect cytoskeletal filaments to each other and to junctional complexes

A

plectin

183
Q

additional filament system; forms ring and cage-like structures; act as scaffolds to compartmentalize membranes into distinct domains

A

septins

184
Q

septin genes in humans

A

13

185
Q

relies on the coordinated deployment of the components and processes

A

cell migration

186
Q

bone cells that migrate through connective tissues

A

fibroblast

186
Q

cells responsible for bone remodeling and renewal

A

osteoclasts

187
Q

plasma membrane is pushed out at the front of the cell; relies on forces generated by
actin polymerization

A

protrusion

188
Q

actin cytoskeleton connects across the plasma membrane to the substratum

A

attachment

189
Q

the bulk of the trailing cytoplasm is drawn forward

A

traction

190
Q

formed by migrating growth cones of neurons and some type of fibroblast; one-dimensional; contain a core of long, bundled actin filaments

A

filopodia

191
Q

formed by epithelial cells and fibroblast; two-dimensional sheet-like structures; contain a cross-linked mesh of actin filaments

A

lamellipodia

192
Q

actin-rich protrusion; three-dimensional; important for cells to cross tissue barriers

A

invadopodia and podosomes

193
Q

depends on hydrostatic pressure within the cell; generated by the contraction of actin and myosin

A

blebbing

194
Q

abundant keratin filaments; epithelial cells of the epidermis of fish and frogs

A

keratocytes

195
Q

assembling at the front and disassembling at the back

A

treadmilling

196
Q

binds preferentially to actin filaments containing ADP-actin; new T-form filaments generated at the leading edge resistant to depolymerization

A

cofilin

197
Q

dynamic assemblies of structural and signaling proteins

A

focal adhesions

198
Q

disengaged interaction between actin network and focal adhesions, polymerization pressure at the leading edge and myosin-dependent contraction cause the actin network to slip back

A

retrograde-flow

199
Q

the front end of the cell remain structurally and functionally distinct from the back end

A

cell migration

200
Q

cytoskeletal coordination takes the form of the establishment of

A

cell polarity

201
Q

activated Cdc42

A

WASp proteins family

202
Q

severe form of immunodeficiency in which immune systems cells have abnormal
actin-based motility and platelets do not form normally

A

Wiskott-Aldrich Syndrome

203
Q

activates the WASp family members; activates the cross-linking activity of the gel-forming protein filamin and inhibits the contractile activity of the motor protein myosin II

A

Rac-GTP

204
Q

turns on formin proteins to construct parallel actin bundles; activates a protein kinase that in indirectly inhibits the activity of cofilin, leading to actin filament stabilization

A

Rho-GTP

205
Q

the movement of a cell toward or away from a source of some diffusible chemical

A

chemotaxis

206
Q

chemotaxis acts through _________ set up large-scale cell polarity

A

Rho family proteins

207
Q

cells that moves toward a source of bacterial infection

A

neutrophils

208
Q

two processes directly inhibit each other;

A