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CBIO3400 > Intermediate Filaments > Flashcards

Intermediate Filaments Flashcards

1
Q

stucture of intermediate filaments

A

polymers

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2
Q

diameter of intermediate filaments

A

10nm

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3
Q

number of genes encode intermediate filaments

A

70 genes

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4
Q

polarity of intermediate filaments

A

intermediate filaments not polarized

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5
Q

overall structure of intermediate filament dimer: N-terminus to C-terminus

A

N’ -Head - Rod - Tail - C’

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6
Q

domain of IF proteins conserved

A

rod domain

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7
Q

IF N’ and C’ domains makes the dimer:

A

polarized

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8
Q

structure of IF rod domain

A

alpha-helical, coiled-coil structure

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9
Q

alpha-helix in rod domain characterized by:

A

heptad repeat sequence

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10
Q

type of IF residues help back two proteins together

A

hydrophobic residues

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11
Q

IF rod domain has hydrophobic residues at positions:

A

hydrophobic residues at positions 1 and 4

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12
Q

fashion in which IF dimers associate with other dimers

A

anti-parallel fashion

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13
Q

tetramers symetric structure makes them:

A

not polar

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14
Q

basic building blocks of intermediate filaments

A

IF tetramers

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15
Q

forms when tetramers assemble end to end

A

protofilament

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16
Q

this forms when four protofilaments assemble

A

protofibril

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17
Q

four protofibrils assemble into:

A

10nm IF

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18
Q

number of interlocked protofilaments IF contains

A

16 protofilaments

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19
Q

number of protofilaments assemble into a protofibril

A

four protofilaments

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20
Q

number of protofibrils assemble into the 10nm IF

A

four protofibrils

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21
Q

IFs are more stable than:

A

microfilaments or microtubules

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22
Q

IFs are more stable than microfilaments or microtubules but are still:

A

dynamic

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23
Q

experiments proves dynamic nature of IFs: this labeled monomer injected into fibroblasts

A

keratin monomer injected into fibroblasts

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24
Q

IFs assemble and dissemble in order of:

A

hours

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25
Q

Class I intermediate filament protein type

A

acidic

26
Q

Class I intermediate filament distribution

A

epithelial cells

27
Q

Class II intermediate filament protein type

A

basic keratins

28
Q

Class II intermediate filament distribution

A

epithelial cells

29
Q

Class III intermediate filament protein type:

A

Desmin, GFP, vimentin

30
Q

Class III intermediate filament distribution

A

muscle, glial cells, mesenchymal cells

31
Q

Class IV intermediate filament protein type

A

neurofilaments

32
Q

Class IV intermediate filament distribution

A

neurons

33
Q

Class V interpediate filament protein type

A

laminins

34
Q

Class V intermediate filament distribution

A

nucleus

35
Q

IF disease: skin gets blistered

A

epidermolysis bullosa simplex

36
Q

keratin 14 forms deterodimers with:

A

keratin 4

37
Q

keratin 14 forms heterodimer with keratin 4 in:

A

basal cells of epidermis

38
Q

keratin 14 and keratin 4 assemble into:

A

protofilaments

39
Q

in mature cell keratin 4 and 14 replaced by:

A

keratin 1 and 10

40
Q

epidermolysis bullosa simplex: keratin 14 and keratin 4 heterodimers cannot form tetramers or protofilaments when:

A

keratin 14 lacks N- or C- terminal domain

41
Q

epidermolysis bullosa simplex: this lacks N- or C- terminal domain

A

keratin 14

42
Q

epidermolysis bullosa simplex: these are fragile and unable to withstand abrasion

A

basal cells of epidermis

43
Q

epidermolysis bullosa simplex: absence of K14/K4 protofilaments seperates:

A

epidermis from dermis

44
Q

epidermolysis bullosa simplex: caused by epidermis seperating from dermis

A

blisters

45
Q

IF disease caused by mutations in LMNA:

A

Hutchinson-Guilford progeria

46
Q

Hutchinson-Guilford progeria caused by:

A

spontaneuous dominant mutations in Lamin A gene (LMNA)

47
Q

Hutchinson-Guilford progeria: mutations in single base activates:

A

cryptic splice site

48
Q

Hutchinson-Guilford progeria: mutation produces:

A

truncated Lamin A protein

49
Q

truncated Lamin A protein called:

A

progerin

50
Q

premature aging disorder

A

Hutchinson-Guilford progeria

51
Q

S/S of Hutchinson-Guilford progeria:

A

baldness, pinched noses, aged skin, dwarfism, craniofacial defects

52
Q

Hutchinson-Guilford progeria: cell part has abnormal morphology

A

nuclear membrane

53
Q

Hutchinson-Guilford progeria: tissues with high levels of stress (like heart) undergo death due to:

A

nuclear instability

54
Q

Lamin A synthesized as:

A

large precursor protein

55
Q

Lamin A large precursor protein modified by addition of:

A

farnesyl group (lipid)

56
Q

farnesyl modification common in proteins localized to:

A

membranes

57
Q

cleaves Lamin A precursor at site of farnesyltation before release

A

Rce

58
Q

Hutchinson-Guilford progeria: farnesyl modification last step being blocked leads to accumulation of intermediate in:

A

nuclei (which is cytotoxic

59
Q

Hutchinson-Guilford progeria: farnesyl modification intermediate deforms:

A

nuclei

60
Q

Hutchinson-Guilford progeria: type of drugs used to treat disease

A

farnesyl transferase inhibitors (FTIs)

CBIO3400 (8 decks)

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