Cytoskeleton Motors Flashcards

(21 cards)

1
Q

What are motor proteins?

A

Mechanochemical enzymes that convert chemical energy (ATP hydrolysis) into mechanical movement

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2
Q

What are the key roles of myosins?

A

Organelle transport.
Muscle contraction.
Cell migration

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3
Q

How does myosin move along actin filaments?

A

ATP hydrolysis causes conformational changes, enabling the myosin head to “walk” along actin.

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4
Q

What is the five step cycle in the movement of actin filametns?

A

1️ATP binding → Myosin releases actin.
2️ ATP hydrolysis → Myosin “cocked” state, storing elastic energy.
3️ Actin binding → Myosin attaches to actin filament.
4️ Power stroke → Pi release triggers forceful actin movement.
5️ ADP release → Myosin remains bound until ATP binds again.

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5
Q

Why does myosin cause rigor mortis in death?

A

Without ATP, myosin heads remain tightly bound to actin, causing muscle stiffness

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6
Q

What is the sarcomere?

A

The contractile unit of muscle fibers, composed of actin & myosin filaments.

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7
Q

What are the key regions in a sarcomere?

A

Z-disk: Anchors (+)-end actin filaments.
I-band: Actin filaments not overlapped with myosin.
A-band: Myosin filaments interdigitate with actin.

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8
Q

How does muscle contraction occur?

A

Myosin walks toward the (+)-end of actin filaments.
Z-disks are pulled inward, shortening the sarcomere.
Each sarcomere contracts equivalently, driving whole muscle fibre contraction.

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9
Q

What is the role of tropomyosin (TM) & troponin (TN)?

A

Tropomyosin blocks myosin-binding sites on actin.
Troponin controls tropomyosin position based on Ca²⁺ concentration.

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10
Q
A
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11
Q

What medical conditions are linked to TN & TM mutations?

A

Cardiomyopathies (heart muscle disorders)

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12
Q

How are heart attacks diagnosed using troponin?

A

Cardiac ischemia (low oxygen) → heart cell death → release of troponin into the bloodstream.
Elevated cardiac-specific troponin levels indicate heart attack severity.

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13
Q

What is kinesin?

A

A microtubule-based motor protein that uses ATP hydrolysis to move toward the (+) end of microtubules

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14
Q

How many kinesin families exist?

A

14 distinct families, with 45 kinesin genes in humans

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15
Q

How does Kinesin-1 move cargo?

A

ATP binding causes conformational changes.
Kinesin “walks” down microtubules in a hand-over-hand fashion.
Cargo is bound to kinesin’s C-terminal domain.

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16
Q

How do dyneins differ from kinesins?

A

Dyneins move toward the (−) end of microtubules, opposite kinesins.
Composed of 1–3 heavy chains, with ATPase motor domains.
Dynein complex is large (1.5 megaDaltons).

17
Q

What are the two families of dyneins?

A

1️Cytoplasmic Dyneins → Transport organelles & vesicles, position nucleus, and assist mitotic spindle formation.
2️ Axonemal Dyneins → Power cilia & flagella beating.

18
Q

How does dynein move?

A

ATP binding detaches dynein from microtubules.
ATP hydrolysis causes attachment & movement.
Release of ADP + Pi triggers the power stroke, shifting microtubule position by 8nm.

19
Q

How does dynein interact with cargo?

A

Dynein binds cargo via the Dynactin complex, which includes:
Arp1 filament (actin-like structure)
Accessory proteins for specific cargo recognition
- BicD protein links dynein to dynactin, ensuring efficient cargo transport.

20
Q

How do microtubules regulate melanosome movement in fish pigment cells?

A

Kinesins disperse melanosomes toward the (+)-end.
Dyneins aggregate melanosomes toward the (-)-end.
Controlled by cyclic AMP (cAMP) → High cAMP = dispersal, Low cAMP = aggregation.

21
Q

How do kinesins & dyneins coordinate transport?

A

Organelles & vesicles use both kinesin & dynein for bidirectional movement.
Dynein moves cargo inward toward the nucleus (−).
Kinesin moves cargo outward to the periphery (+).