The Cytoskeleton Flashcards

1
Q

General features of the cytoskeleton

A

Made of 3 polymers: -microtubules

  • intermediate filaments
  • actin filaments

Useful for:- shaping of the cell

  • intracellular movements
  • cell movement
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2
Q

Structure of actin filaments

A
  • Twisted chain of units of G-actin which makes up the F-actin
  • very thin (7nm)
  • plus and minus end means its polar
  • associated with a bunch of ABPs
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3
Q

What are the three different isoforms of G-actin and where are they found?

A

Alpha - mainly in muscle cells

Beta and gamma - mainly in non-muscle cells

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4
Q

Which end of actin filaments does G-actin get added to?

A

Plus end is more favourable

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5
Q

What two ABPs control the G-actin level?

A

Profilin facilitates actin polymerisation

Thymosin beta-4 presents the addition of actin monomers to F-actin

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6
Q

What do Actin bundling proteins do?

A

Keep the F-actin in parallel bundles (like in epithelial cells

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7
Q

What do cross-linking proteins do?

A

Maintain F-actin in a gel-like meshwork- like in the cell cortex under the plasma membrane

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8
Q

What do F-actin severing proteins do?

A

Break F-actin into smaller filaments by adding these proteins at the end of the polymers

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9
Q

What do motor proteins (like myosin) do?

A

Transport vesicles and/or organelles through actin filaments

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10
Q

What are the functions of actin filaments in skeletal muscle cells?

A

Arranged in a para-crystalline array, integrated with different ABPs
Interaction with myosin allows for muscle contraction

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11
Q

What are the functions of actin filaments in non-muscle cells?

A

Forms a thin sheath beneath the plasma membrane

Associated with myosin to form a purse sting result in cleavage of mitotic cells (cytokinesis)

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12
Q

What are the steps to cell migration?

A
  • The cell pushes lamellipodia (plural) or filopodia(single) out at its front (actin polymerisation)
  • these protrusions adhere to the surface (integrins line the actin filaments to the extra cellular matrix surrounding the cell)
  • cell contraction and retraction of the rear part of the cell (interaction between actin filaments and myosin)
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13
Q

What do accessory proteins regulate?

A
  • size and rate of filament formation (nucleation)
  • polymerisation/depolymerisation
  • function
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14
Q

Structure of intermediate filaments

A
  • tough
  • rope-like with many long strands twisted together and made up of many subunits
  • medium size (8-12nm)
  • they form a network through the cytoplasm, joining up cell-cell junctions (desmosomes)
  • withstand mechanical stress when cells are stretched
  • they surround and strengthen the nucleus
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15
Q

What is each monomer of the intermediate filaments made up of?

A
  • N-terminal globular head
  • C- terminal globular tail
  • central elongated rod-like domain
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16
Q

What is a dimer?

A

Two units of an intermediate filaments monomer that is very stable

17
Q

What do two dimers form?

18
Q

What do tetramears look like when they bind to each other?

A

A rope-like filament

19
Q

What are the types of cytoplasmic intermediate filament and and their localisation?

A
  • keratin(in epithelia)
  • vimentin and vimentin-related (in connective tissue, muscle and neurological cells)
  • neurofilaments (in nerve cells)
20
Q

What is the nuclear intermediate filament and and its localisation?

A

Nuclear lamins (in all nucleated cells)

21
Q

What does IFBP stand for?

A

Intermediate filament binding proteins

22
Q

Examples of IFBPs

A

Fillagrin binds keratin filaments into bundles
Synamin and plectin bind desmin and vimentin
Plakins keep the contact between the desmosomes of epithelial cells

23
Q

What are the functions of the IF in the cytoplasm?

A
  • tensile strength enables the cells to stretch
  • provides structural support by creating a deformable 3D structural framework and reinforcing cell shape and fixing the organelle localisation
24
Q

Functions of the IF in the nucleus

A
  • forms a mesh rather than a rope like structure
  • lines the inner face of the nuclear envelope to strengthen it and provides attachment sites for chromatin
  • disassembles and reforms at each cell division as the nuclear envelope disintergrates (unstable). This is controlled by post-translational modifications (mainly phosphorylation and dephosphorylation)
25
Give the structure of microtubules
-hollow tubes made up of the protein tubulin -relatively stiff (25nm) -each filament is polarised (has a head/tail direction) - it has a dynamic structure: =it can assemble and disassemble in response to cell needs
26
How can microtubules assemble/ disassemble in response to cell needs?
Tubulin in cell B is roughly 50:50 as free or in filament.
27
What does MTOC stand for and what is it?
MicroTubule Organising Centre | Specialised protein complexes where assembly of tubulin unit starts
28
What is the MTOC in most cells and how does it work?
The centrosome. It contains a gamma tubulin ring that initiates the microtubule growth
29
What makes up the microtubule?
Heterodimers of alpha and beta tubulin
30
What is polarised growth and does it happen in microtubules
There is one end that grows after than the other- yes it does
31
Give the functions of microtubules
- intracellular transport (act like railway tracks on which molecules can run. There are different motors for different molecules and the directionality of filaments is vital) - organises position of organelles (which provides the polarisation of cells) - rhythmic beating of the flagella
32
How does the beating of cilia and flagella happen?
- core consists of 9 pairs of microtubules around two central microtubules (called an axoneme) - bending of cilia and flagella is driven by dynein (a motor protein) - the basal body (at the bas of the tubule) controls the assembly of the axoneme