Microtubules Flashcards

1
Q

chemical property of microtubules

A

polarized

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2
Q

microtubules oriented with + ends toward:

A

plasma membrane

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3
Q

microtubules oriented with - ends towards:

A

centrosome

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4
Q

4 functions of microtubules:

A

mitosis, transport, motility, signaling

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5
Q

microtubules are composed of these subunits

A

alpha- and beta- tubulin dimers

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6
Q

each MT tubulin monomer can bind:

A

1 GTP

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7
Q

GTP bound to this tubulin is physically trapped at dimer interface and is never hydrolyzed or exchanged

A

alpha-tubulin

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8
Q

tubulin type can bind either GTP or GDP

A

beta-tubulin

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9
Q

one tubulin MT subunit consists of:

A

tubulin heterodimer

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10
Q

tubulin heterodimers assemble linearly to form:

A

protofilament

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11
Q

13 protofilaments form:

A

microtubule

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12
Q

structure of microtubule

A

hollow tube

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13
Q

drug stabilizes MTs

A

Taxol

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14
Q

drug binds and stabilizes actin filaments

A

Phalloidin

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15
Q

drug caps filament plus ends and destabilizes microfilaments

A

Cytochalasin

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16
Q

drug severs actin filaments

A

Swinholide

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17
Q

multiple subunits associating laterally important for allowing cytoskeletal filaments to:

A

resist breakage

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18
Q

for assembly of MTs, tubulin concentration must be:

A

above Cc

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19
Q

for MTs to depolymerize, tubulin concentration must be:

A

below Cc

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20
Q

end that tubulin alpha-beta-dimers add more rapidly

A

+ end

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21
Q

Preferred end for assembly is the (+) end, in which this tubulin is exposed

A

beta tubulin

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22
Q

Cc is lower at this MT end

A

+ end

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23
Q

GTP bound to beta-tubulin hydrolyzes during

A

polymerization

24
Q

Free energy from hydrolysis is transferred to polymer, making dissociation of this form of tubulin more energetically favorable

A

D-form

25
Q

soluble tubulin subunits are in this form

A

D-form

26
Q

MTs have GTP cap at this end

A

+ end

27
Q

Cc is when:

A

on rate = off rate

28
Q

this tubulin subunit form has higher affinity for GTP-tubulin

A

T form

29
Q

this tubulin form has higher Cc

A

D form

30
Q

dissociation of subunits preffered on this end at intermediate concentration

A
  • end
31
Q

dissociation of tubulin dimers is favored at this end because Cc T is lower than intermediate concentrations

A

+ end

32
Q

name for MT movement in live cells

A

treadmilling

33
Q

to visualize treadmilling, small amount of this injected into cell

A

rhodamine conjugated tubulin

34
Q

describes the assembly, catastrophe, disassembly, and rescue of MTs

A

dynamic instability

35
Q

dynamic instability depends on:

A

GTP cap

36
Q

GTP cap removal from + in results in reduced affinity for:

A

Tubulin-GTP (T form)

37
Q

during this stage of dynamic instability, subunits lost from + end and local tubulin subunit concentration increases

A

dissasembly

38
Q

during this stage of dynamic instability, free tubulin-GTP reaches Cc of D form

A

rescue

39
Q

these proteins stabilize MTs

A

MAPs

40
Q

3 types of MAPs

A

tau, MAP2, MAP4

41
Q

MAPs bind:

A

charged wall of MT

42
Q

MAP type found only in dendrites

A

MAP2

43
Q

MAP type forms fibrous cross-bridges between MTs and links to IFs

A

MAP2

44
Q

MAP type is present on both dendrites and axons

A

Tau

45
Q

MAPs are regulated by:

A

phosphorylation

46
Q

these control MAP activity

A

MARK/Par-1 and CDK

47
Q

cell with overexpression of this MAP have larger diamer and MTs more spaced apart

A

MAP2

48
Q

these proteins bind to the + end of MTs

A

+TIP

49
Q

MT protein binds seam at + end and acts as “weld”

A

EB1

50
Q

proteins enhance MT catastrophes by enhancing GTP hydrolysis at + end

A

Op18/Stathmin

51
Q

inactivates Op18/Stathmin

A

phosphorylation

52
Q

organizes MTs throughout the cell

A

centrosome

53
Q

centrosome consists of:

A

two centrioles and pericentriolar material

54
Q

pericentriolar material contains:

A

gamma-TURC (Tubulin Ring Complex)

55
Q

serves as nucleation site for MT filaments

A

gamma-TURC

56
Q

centrosome (MTOC) is located at:

A

center of cell (near nucleus)

57
Q

gamma-TURC located at this end of MT

A
  • end