Contractile Proteins Flashcards

(37 cards)

1
Q

which type of actin has polarity: globular or filamentous?

A

filamentous

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2
Q

actin bundles

A

cross-linked actin into closely packed parallel arrays

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3
Q

actin networks

A

loosely cross-linked actin into orthogonal arrays that form 3D meshworks with gel-like properties
- more flexible

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4
Q

actin-bundling proteins

A

small, ridged proteins that force the filaments to align closely with each other

  • cross-links actin
  • determines the nature of association of filaments
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5
Q

fimbrin

A

actin-bundling protein; binds to actin filaments as a monomer; holds two parallel filaments closely together
- ex: microvilli

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6
Q

contractile bundles of actin

A

loosely bundled actin

- ex: contractile ring used in mitosis

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7
Q

alpha-actinin

A

actin bundling protein; allows motor protein (myosin) to interact during contraction; binds as a dimer; filaments of actin are separated by a greater distance which allows myosin to interact during contraction

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8
Q

filamin

A

actin bundling protein; binds actin as a dimer; can create 3D meshwork

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9
Q

spectrin

A

actin binding protein in RBCs; forms actin network that forms a cortical cytoskeleton; this network interacts with membrane proteins via interactions with ankyrin, protein 4.1

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10
Q

hereditary spherocytosis

A

decrease flexibility and stability of RBCs; caused by mutations in the cortical cytoskeleton proteins in RBCs (spectrin, ankyrin, 4.1)
- Sx: jaundice, anemia, splenomegaly

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11
Q

pseudopodia

A

type of actin projection that is responsible for phagocytosis

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12
Q

lamellipodia

A

broad, sheet like extensions of actin at the leading edge of a moving cell

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13
Q

filopodia

A

thin projections of plasma membrane supported by actin bundles; formation and retraction of filopodia is based on regulated assembly and disassembly of actin filaments

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14
Q

what driving force allows myosin to move along actin filaments

A

ATP hydrolysis

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15
Q

head domain of myosin

- two parts

A

contains actin binding and ATP binding sites; ATPase activity

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16
Q

neck domain of myosin

A

the flexible region; binds myosin light chain peptides

17
Q

tail domain of myosin

A

intertwines to bring myosin head regions in close proximity; binds membranes and organelles

18
Q

skeletal muscle myosin I

  • neck size
  • function
A
  • 10-14 (small)

- interacting with membranes, endocytosis

19
Q

skeletal muscle myosin II

  • neck size
  • function
A
  • 8 nm (v small)

- skeletal muscle contraction

20
Q

skeletal muscle myosin V

  • neck size
  • function
A
  • 36 nm (v long)

- organelle transport

21
Q

how does rigor mortis occur

A

absence of ATP in the muscle –> myosin attaches to actin filaments and contracts and cannot relax

22
Q

what happens when ATP binds to myosin

A

a conformational change occurs causing release of actin; myosin then remains in “cocked state” –> binds to actin causing release of Pi (energy) –> “power stroke”

23
Q

“power stroke” of myosin bound to actin

A

release of P and i elastic energy which straightens myosin; moves actin filaments to the left

24
Q

as length of neck domain of myosin increases, ____

A

rate of movement increases

25
what form is myosin in during low Ca2+ environements
folded
26
what phosphorylates myosin
MLC (myosin light chain) kinase
27
phosphorylation of myosin by MLC kinase causes ___
unfolding and activation of myosin
28
what activates MLC kinase
calcium
29
what dephosphorylates myosin
MLC (myosin light chain) phosphatase
30
dephosphorylation of myosin causes
folding and relaxation of myosin (inactive)
31
what causes the cleavage furrow in cytokinesis
myosin movement along actin filaments
32
difference between myosin VI and myosin V in moving across filamentous actin
myosin VI moves towards the (-) end | myosin V moves towards the (+) end
33
difference between dynein and kinesin in moving across filamentous actin
dynein moves toward (-) end | kinesin moves toward (+) end
34
Duchenne Muscular Dystrophy - type of disorder - what is it
- X-linked recessive | - progressive muscle wasting due to mutations within dystrophin gene
35
in-frame mutations in the dystrophin gene cause
becker muscular dystrophy
36
out of frame mutations in the dystrophin gene cause
duchenne muscular dystrophy
37
function of dystrophin
connects cytoskeleton to basal lamina; stabilizes the membrane of muscle cells