Exam 4 - Lecture 7 Flashcards

1
Q

The cytoskeleton is a_______and plays a role in _______? Two features are_________.

A

network of
interconnected filaments and tubules
extending through the cytosol
 It plays roles in cell movement and division
 It is dynamic and changeable

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2
Q

The major structural
elements of the
cytoskeleton are

A

Microtubules
 Microfilaments
 Intermediate
filaments

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3
Q

Microtubules are
composed of

A

tubulin
subunits and are about
25 nm in diameter

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4
Q

Microfilaments subunits and size

A

7 nm
wide, are composed of
actin subunits

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5
Q

Intermediate filaments
-size and composition

A

8–12 nm, are variable in
composition

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6
Q

what is a Mechanically Integrated Structure

A

cytoskeleton

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7
Q

MTs resist

A

bending when a cell is compressed

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8
Q

MFs serve as

A

contractile elements that generate tension

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9
Q

IFs are

A

elastic and can withstand tensile forces

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10
Q

connect IFs, MFs, and MTs

A

linker proteins

Example: plectin, found at sites
where intermediate filaments connect to Mts and MTF

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11
Q

the largest structural
elements of the cytoskeleton

A

Microtubules (MTs)
 They are involved in a variety of functions in the
cell

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12
Q

what are the two main types of microtubules

A

Cytoplasmic microtubules

Axonemal microtubules

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13
Q

Cytoplasmic microtubules

A

pervade the cytosol and
are responsible for a variety of functions:
 Formation of mitotic and meiotic spindles
 Maintaining or altering cell shape
 Placement and movement of vesicles

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14
Q

Axonemal microtubules

A

Axonemal microtubules include the organized and
stable microtubules found in structures such as Cilia
and Flagella

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15
Q

Describe the strucutre of MTs

A

MTs are straight, hollow cylinders of varied length that consist of
longitudinal arrays of polymers called protofilaments
 The basic subunit of a protofilament is a heterodimer of tubulin, one
α-tubulin and one β-tubulin
 These bind non-covalently to form an αβ-heterodimer, which does
not normally dissociate
 Microtubules can form as Singlets, Doublets, or Triplets

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16
Q

Describe Microtubule Assembly Graph

A

MT formation is slow at first
because the process of
nucleation is slow; this period
is known as the lag phase
 The elongation phase is
much faster
 Plateau phase: the mass of
MTs reaches a point where the
amount of free tubulin is
diminished.

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17
Q

Describe the lag phase of MT assembly

A

MT formation is slow at first
because the process of
nucleation is slow; this period
is known as the lag phase

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18
Q

Drugs Affecting Cytoskeleton

A

Colchicine
Nocodazole

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19
Q

Colchicine

A

binds to tubulin monomers, inhibiting their assembly into MTs
and promoting MT disassembly
 Vinblastine, vincristine are related compounds

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20
Q

Nocodazole

A

inhibits MT assembly, and its effects are more easily reversed
than those of colchicine

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21
Q

MTs originate from

A

a microtubule-organizing
center (MTOC)

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22
Q

Many cells have an MTOC called a

A

centrosome near the nucleus

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23
Q

In animal cells, the centrosome is associated
with

A

two centrioles surrounded by
pericentriolar material

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24
Q

Centriole walls are formed by

A

9 pairs of triplet
microtubules
 oriented at right angles to each other
 involved in basal body formation for cilia and flagella
 cells without centrioles have poorly organized mitotic
spindles

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25
describe γ-Tubulin
Centrosomes have large ring-shaped protein complexes in them; these contain γ-tubulin  γ-tubulin is found only in centrosomes
26
proteins promote depolarization of MTs
Stathmin/Op18 Catastrophins
27
Microtubule Stability - MAPs
Cells regulate MTs with great precision  Others regulate MT structure  MAPs, microtubule-associated proteins, bind along a microtubule wall, allowing for interaction with other cellular structures and filaments
28
Some MT-binding proteins use ATP to
to drive vesicle or organelle transport or to generate sliding forces between MTs
29
Stathmin/Op18
depolarizes MTs by binding to tubulin heterodimers and prevents their polymerization
30
Catastrophins
depolarizes Mts by acting at the ends of MTs and promote the peeling of subunits from the ends
31
Microfilaments 1. size 2. best known role 3. 3 main involvements
are the smallest of the cytoskeletal filaments  Best known for their role in muscle contraction  Involved in cell migration, amoeboid movement, and cytoplasmic streaming
32
What is actin? What are the various types?
the Protein Building Block of Microfilamens Actin is a very abundant protein in all eukaryotic cells  Actins can be broadly divided into muscle-specific actins (α-actins) and nonmuscle actins (β- and γ-actins)
33
actin assembly
Once synthesized, it folds into a globular-shaped molecule that can bind ATP or ADP (G- actin; globular actin)  G-actin molecules polymerize to form microfilaments: F-actin  All the actin monomers in the filament have the same orientation
34
Drugs Affecting Microfilaments
Cytochalasins Latrunculin A
35
Cytochalasins
are fungal metabolites that prevent the addition of new monomers to existing MFs
36
Latrunculin A
is a toxin that sequesters actin monomers and prevents their addition to MFs
37
Actin-Binding Proteins role + example
Actin-binding proteins: used by cells to precisely control where actin assembles and the structure of the resulting network  Example: Capping proteins bind the ends of a filament to prevent further loss or addition of subunits
38
Microvilli
Actin bundles in microvilli are the best-studied examples of ordered actin structures  Microvilli are prominent features of intestinal mucosal cells; they increase the surface area of the cells  The core of a microvillus consists of a tight bundle of MFs with the ends pointed toward the tip
39
Intermediate filaments (IFs) where are they found? Common example stability and solubility? important function
are not found in cytosol of plant cells but are abundant in many animal cells  An IF is keratin, an important component of structures that grow from skin in animals  IFs are the most stable and least soluble components of the cytoskeleton  They likely support the entire cytoskeleton
40
what is unique about IF proteins
IF Proteins Are Tissue Specific IFs differ greatly in amino acid composition from tissue to tissue
41
6 classes of IFs
class 1 - 6
42
describe class 1
Class I: acidic keratins
43
describe class 2
Class II: basic or neutral keratins * Proteins of classes I and II make up the keratins found in epithelial surfaces covering the body and lining its cavities
44
class 3
connective tissue, muscle cells, and glial cells
45
class 4
nerve cells
46
class 5
inner surface of the nuclear membrane
47
class 6
nerve cells of embryos
48
IF assembly
The fundamental subunits of IF proteins are dimers  IF proteins are fibrous rather than globular  Each has a homologous central rodlike domain  Flanking the central helical domain are N- and C- terminal domains that differ greatly among IF proteins IFs Assembly  Two IF polypeptides intertwined into a coiled-coil  Two dimers align laterally to form a tetrameric protofilament  Protofilaments overlap to build up a filamentous structure about eight protofilaments thick
49
Cell motility can be
Movement of a cell or organism through the environment  Movement of the environment past or through a cell  Movement of components in the cel
50
Contractility
used to describe shortening of muscle cells, is a specialized form of motility
51
Two Eukaryotic Motility Systems
Microtubule-based motility Microfilament-based motility
52
Microtubule-based motility example
examples: fast axonal transport in neurons; the sliding of MTs in cilia and flagella
53
Microfilament-based motility example
Example: muscle contraction
54
Microtubule-Based Movement Inside Cell requires what two proteins and whaat is the role of MT
Kinesins and Dyneins MTs provide a rigid set of tracks for transport of a variety of organelles and vesicles
55
Microtubule-associated motor proteins...
Microtubule-associated motor proteins—kinesins and dyneins—walk along the MTs and provide the force needed for movemen
56
Kinesin I
is involved in ATP-dependent transport toward the plus ends (away from the centrosome), called anterograde axonal transport
57
Cytoplasmic dynein
moves particles (cargo) in the opposite direction, called retrograde axonal transport
58
Kinesin Movement Along MTs
Kinesin movement looks like “walking,” with the two globular head domains taking turns as the front foot  It can move long distances along an MT before detaching from it by releasing bound ADP and acquiring a new ATP, so that the cycle repeats
59
ATP-dependent motors, the large superfamily called
myosins
60
ATP-dependent motors =
myosins the large superfamily myosins, interact with and exert force on actin microfilaments  Currently there are 24 known classes of myosins
61
Myosin Functions
Myosins function in a wide range of cellular events, including  Muscle contraction  Cell movement  Phagocytosis  Vesicle transport
62
Muscle contraction
is the most familiar example of mechanical work mediated by intracellular filaments
63
Mammals have what types of muscle
skeletal, cardiac, and smooth muscle
64
Skeletal Muscle Cells contain what two filaments?
muscle fibers contain thin filaments containing actin and thick filaments containing myosin
65
Thick Filaments
Each thick filament consists of hundreds of molecules of myosin, oriented in opposite directions in the two halves of the filament  The myosin is arranged in staggered fashion  Protruding heads of myosin molecules contact the adjacent thin filaments, forming cross-bridges
66
Thin Filamentsand the three proteins it contains
Thin filaments interdigitate (interlock) with the thick filaments  Thin filaments contain three proteins: F-actin, intertwined with tropomyosin and troponin
67
The Sliding-Filament Model Explains Muscle Contraction
The sliding filament model was proposed in 1954  According to the model, muscle contraction is due to thin filaments sliding past thick filaments, with no change in length of either
68
give some functions of MTs, MFS, IF
MT ( varies per type, but Axonemal = cell motility, and cytosoolic varies) MF - muscle contractions, cell locomotion, cyoplasmic steaming, cell shape, intracellulat transport IF - structural support, animal cell shape, stregth of nerve cell axons