Lecture 3 Flashcards

0
Q

Mreb

A
  • prokaryotic ancestor of actin

- give rod-shaped bacteria structure

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1
Q

Microfilaments

A
  • made up of actin (alpha muscle, beta/gamma non)
  • abundant in all tpyes of eukaryotic cells
  • 4 muscle, 2 non
  • actin is highly conserved
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2
Q

Cytochalasins

A
  • bind to barbed end
  • block elongation
  • can inhibit mitosis
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3
Q

Phalloidin

A
  • prevents dissociation

- can be labeled with fluorescent dyes

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4
Q

Spectrin

A
  • found in RBCs
  • binds cortical cytoskeleton to plasma membrane
  • ghost RBCs after bursting
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5
Q

Dstrophin

A
  • binds cortical cytoskeleton to plasma membrane

- muscular dystrophy gets name from this

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6
Q

Villin and Fimbrin

A

-cross-links in microvilli

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7
Q

Caalmodulin and Myosin 1

A

-cross-links actin to plasma membrane in microvilli

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8
Q

alpha-actinin

A
  • cross-links stress fibers and connects actin to protein-plasma membrane copes
  • adaptor for integrins to interact with F-actin
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9
Q

Filamin

A
  • cross-links actin at wide angles to form screen-like gels
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10
Q

Thymosin

A
  • controls treadmilling

- captures actin monomers and prevents from being polyerized

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11
Q

Profilin

A
  • binds to actin monomers, prevents polymerization
  • controls treadmilling
  • facilitates exchange of bound ADP for ATP
  • *only ATP-actin monomers can assemble into F-actin
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12
Q

Gelsolin

A
  • controls treadmilling
  • destabilizes F-actin and caps filaments, prevents loss and addition of G-actin
  • in presence of Ca, fragments actin filament and remains bound to plus end
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13
Q

Cofilin

A
  • controls tread

- triggers depolymerization of ADP-bound actin at minus end

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14
Q

Arp 2/3

A
  • initiates growth of F-actin fro sides of existing filament
  • causes branching
  • nucleation (3 actin monomers coming together) is rate-limiting
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15
Q

Formin

A
  • and Arp 2/3 complex determine where filament are formed
  • large dimers that bind initial monomer, and move along the growing filament
  • nucleate long unbranched actin filaments, many stabilized by tropomyosin
16
Q

Laatrunculins

A
  • bind to G-actin and induce F-actin depolymerization

- non native proteins, used in research to break down filaments

17
Q

Parallel Bundles

A
  • closely spaced actin filaments aligned in parallel

- barbed ends adjacent to plasma membrane

18
Q

Contractile Bundles

A
  • more widely-spaced filaments, cross-linked by alpha-actinin
  • allows motor protein myosin to interact with actin
19
Q

Intermediate Filaments

A
  • abundant in cells subject to mechanical stress
  • provide tensile strength to cells such as neurons and muscle
  • strengthen epithelial cells such as desmo and hemi
  • common monomer consisting of central a-helix rod flanked by head and tail domains
20
Q

Intermediate Assembly

A
  • 2 antiparallel dimers form staggered tetramer
  • form spontaneously, doesn’t require ATP
  • formed by poly of long, rodlike proteins
  • repeated AA segents (heptads)
21
Q

Intermediate Filament Associated Proteins (IFAPs)

A
  • stabilize filament
  • may cap to prevent further elongation
  • filaggrin, epinemin, paranemin, plectin, synemin
22
Q

Intermediate Filament Types

A
  • Type I: acidic keratins, associaed with plaques of desmo and hemi
  • Type II: neutral to basic keratins
  • Type IV: neurofilaments, axons and dendrites
  • Type V: nuclear lamins, mechanical support for nuclear envelope
  • Type VI: nestin, associated with CNS stem cells
23
Q

Microtulues

A
  • thick, composed of tubulin dimers
  • consist of 13 protofilaments
  • plus end grows more rapidly in presence of low Ca
24
Q

Factors Inhibiting Microtubule Polymerization

A
  • colchicines, used to create karyotype
  • colcemid
  • vincristine and vinblastin, anti-cancer
  • taxol stabilize
25
Q

Cilium Structure

A
  • 9 peripheral doublets + central pair of microtubules

- each doublet has alpha tubule (13 protofilaments) and beta (10-11)

26
Q

Fatty Acid Characteristics

A
  • long-chain pack well together and limit movment
  • short are more limited but create spaces which other chains can move
  • saturated has no double bonds, max H+
27
Q

Outer Leaflet of Phospholipid bilayer

A
  • Cholesterol
  • phosphatidylcholine
  • sphingomyelin
28
Q

Inner Leaflet of Phospholipid bilayer

A
  • cholesterol, phosphatidylethanolamine, phosphatidylserine (- charge)
  • phosphatidylinositol, - charge, important in cell signaling, only in inner
29
Q

Glycolipids

A

-outer leaflet with carbohydrate portion facing extracellular, forms glycocalyx

30
Q

Cholesterol

A
  • High temps, interfers with FA chain movement, makes membrane less fluid, reduced permeability to small molecules
  • low temps, prevents membranes form freezing
31
Q

Glycocalyx

A
  • not integral part of membrane

- carb coat composed of carb portions of glycolipids and glycoproteins

32
Q

Lipid Rafts

A
  • small patches of cholesterol and sphingolipids

- no proteins, smooth surface

33
Q

Peripheral Proteins

A

-can be removed by altering pH or ionic content of environment

34
Q

Integral Proteins

A
  • Embedded, extracellular portion typically glycolsylated

- can only be removed by detergents

35
Q

Transmembrane Proteins

A
  • integral that pass completely through both layers
  • channel or transporter proteins
  • 1 hydrophobic and 2 philic domains
  • membrane-spanning portions usually a helix with 20-25 hydrophobic AA (glycophorin, band 3 anion tranporter for Cl ions)
36
Q

Single Pass Transmembrane Proteins

A
  • single hydrophobic domain passes through layer only once
  • enzyme-like receptrors (receptor tyrosine kinases)
  • glycophorin (RBC membranes)
37
Q

Multiple-pass Transmembrane Proteins

A
  • use two or more hydrophobic domains
  • activated by add of phosphate
  • G-protein-linked receptors (7 trans domains)
  • Large transporter and channel proteins (porin has 12 trans domains as does glucose)