Cytoskeleton I Flashcards

1
Q

Roles of cytoskeleton

A

Cell polarity

Directional migration

Formation of mitotic/meiotic spindle

Chromasome seg

cytokinesis

Intracellular transport, exo/endo cytosis

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2
Q

Why do cytoskeletal components have dif distributions

A

Important for cell shape, polarity, and tissue formation

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3
Q

What are cytoskeletal structure made of

A
Small protein subunits
Noncovalent polymers
Dynamic
Accessory proteins regulate sites and state of assembly
Adaptable
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4
Q

Intermediate filaments key facts

A

Intermeidate in size, more stable

Major components of cytoskel and nuclear boundary

Protection from mechanical stress-within cells (surround nun and extend to periphery) and at junction of cell and ECM

Role insignalling and gene reg networks

No motor

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5
Q

Intermediate filaments strucutre

A

Include keratins, near filaments, nuclear lamins

Two chained coiled coil that assembles to form tetramere-tetramer forms higher order assemblies-held together by hydrophobic interactions

N anC terminal ends are globular-coiled coil region interrupted by linker domains

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6
Q

Intermediate protein assembly

A

Antiparallel tetrameters

not polar

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7
Q

Actin key facts

A

Polyermeric and globular (g-actin)

Polar-ends are distinctly different

Bound nucleotide (ATP/ADP)

Plus end (barbed) is fast growing
Minus end (pointed) is slower growing)

Helical filament

Binding proteins modify filament dynamics and higher order assemblies

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8
Q

Actin elongation

A

Faster at plus (barbed) end

Rate limiting step is formation of nucleus (3 subunits)

ATP actin is preferentially added to barbed end
-hydrolysis not required for polyermaization-bound nun influences stability

Each actin filament has ADP-actin, except for extreme barbed end

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9
Q

What do proteins that bind to actin do

A

Bind to one end (cap)

Sever filaments

Cross link

Anneal etc

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10
Q

MT and actin filament parallels (6)

A

Both form globular protein by condensation/polymerization mech to form polar structure

Both have pref end of monomer addition

Nuc hydroylsis lags behind polyermization elaving ATP/GTP cap at plus end

Nucleotide at plus end determines stability

Dynamics and state of assembly reg by MT binding proteins

Structures are NOT RELATED

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11
Q

Tubulin and MT structure

A

Two subunits

  • b binds to GTP
  • GTP hydrolyzed during polymerization which is at plus end of molecule
  • polyermerizes to long protofilaments in MT

Polar

Nothing on the inside

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12
Q

Tubulin and MT function

A

Vesicular and organelle transport, from mitotic spindle, cilia, and flagella, entriole and basal bodies

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13
Q

What structures are made of MT’s

A

cilia, flagella, centrioles, and basal bodies

Have knobs coming out of outer doublet (dyenine)

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14
Q

Primary cilium

A

Apparent on most cells

Non-motile
Usually 1 per cell
Sensory organellles
Central player in dev signaling pathways

No central pair, no knobs oming out of outer doublet (no dyeing)

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15
Q

Centrosome Facts

A

MT organizing center-all MT eminate from here

  • Minus end is located here
  • gamma tubulin ring complex that nucleates the 13 protofilaments of MT’s and caps the - ends
  • +ends oriented towards cell periphery
  • centrioles duplicate at beginning of S phase of mitosis
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16
Q

Mitotic spindle

A

Kinetochore attaches to plus end of MT and enables alignment on metaphase plate

Plus ends interact with other plus ends of other centrioles

17
Q

3 types of MT and functions

A

Astral-go in every direction thats not metaphase plate

Kinetochore-attach to kinetochore

Interpolar-attach to other plus ends

18
Q

NTP to NDP

A

Release takes place after polymerization

Results in polarity

Addition is fast on +, slow on -

Nuc cap (with GTP or ATP) at +

GDP or ADP on -

19
Q

T form vs D form

A

NTP or NDP

minus end addition is slow-hydrolysis catches up

Plus end addition is fast-hydrolysis lags behind

20
Q

Dynamic instability

A

Plus end transitions between growth and shrinking

GTP tubulin cap stabilizes plus end

GDP tubulin subinits at the plus end destabilize-rapid depolymerization (catastrophe)

21
Q

MAPS

A

Microtubule Associated Proteins

Regulate state of MT assembly

Stabilize or destabilize plus of minus ends

Bind to side-stabilize by side binding or bundle formation

Sever

22
Q

Tau protein

A

a type of MAP

Connections between microtubules

Tangled in alzheimers

23
Q

When microtubules reach cell periphery

A

+ tip proteins inhibit catastrophes

+tip protein bind and track the + end of growting MT

Communicate and connect with cell cortex to transport materials to cortex and interact with actin cytoskeleton

Capture chromosomes during mitosis-association with kinetochore

24
Q

Phallodin

A

Binds and stabilizes actin filaments

-death angel mushroom

25
Q

Death angel mushroom

A

contains fallopian and amanitin (RNA pol II inhibitor)

26
Q

Colchicine

A

Depolymerizes MTs

27
Q

Taxol

A

Binds and stabilizes MTs

-widely used anti cancer drug-inhibit cell division

28
Q

Cell migration facts

A

Occurs during development-pathfinding and targeting of neurons

Chemotaxis

Tissue formation, repair, remodeling-migration of cells to repair skin won

Cancer-metasis of oncogenic cells

29
Q

Chemotaxis

A

Migration of neutro[hols to sites of infection

30
Q

Cell migration movement of leading and lagging edge

A

Leading edge is driven by actin polymerization

Tail follows with actin-myosin II

31
Q

Cytoskeleton dependent movements

A

Cellular movement can be motor driven or polymerization driven

Intracellular transport can be motor driven or polymerization driven

Pathrgens usurp ceullular machinery

32
Q

Neutrophil chasing bacterium

A

Neutrophils protect body from bacteria that enter body though skin

Chase bacteria by chemotaxis

  • actin poly at leading edge
  • actin and myosin II dependent tail contractions
33
Q

What is role of dynamic actin filaments in cellular functions

A

Actin polyermation alone can drive cell migration

Some bacteria commandeer the cell’s actin polymerization machinery during infection

34
Q

Actin polymerization provides force for movement by

A

Elongation of barded end

Need many growing ends

  • nucleate more actin filaments
  • Sever existing filaments to create more barbed ends
  • Form braces from existing actin filaments

Arp2/3 complex-Nucleates filaments from the sides of actin filaments-make complex branched structures

35
Q

Arp2/3 complex

A

Nucleates filaments from the sides of actin filaments-make complex branched structures

36
Q

Rho dependent signalling cascade

A

Regulates dendritic nucleation

Arp2/3 requires activition for efficient nucleation of branched filaments-nucleated filaments push against cell membrane

Activators-downstream in rho family of small GTP ases signaling cascade

Localizes activation at cell membrane, site of protrusion

37
Q

Arp2/3 dependent polymerization is involved in

A

Neutrophil migration to site of infection

Wound healing

Invasion of metastatic cancer cells

Bacterial infections

endocysosis

many more

38
Q

Listeria

A

Infects epithelial cells-hijacjs Arp2/3 dependent actin polymerization machinery

Actin filaments polymerize-form a tail that propels the bacterium through cytoplasm like a comet