Myosins and Molecular Motors Overview

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Questions and Answers

What is the primary function of kinesins in a cell?

  • To form filaments that support cell structure
  • To produce ATP through mitochondrial respiration
  • To facilitate the process of transcription
  • To generate motion through ATP hydrolysis (correct)

Which type of dynein is primarily responsible for flagella and cilia movement?

  • Mitotic dynein
  • Cytoplasmic dynein
  • Molecular dynein
  • Axonemal dynein (correct)

How do kinesins compare to myosins in terms of motor domain size?

  • Motor domains of kinesins are only found in muscle cells
  • Kinesins have smaller motor domains than myosins (correct)
  • Kinesins have larger motor domains than myosins
  • Kinesins and myosins have motor domains of equal size

What cellular components do kinesins help transport?

<p>Intracellular cargo such as vesicles and proteins (C)</p> Signup and view all the answers

What type of protein is kinesin classified as?

<p>Microtubule-based molecular motor (B)</p> Signup and view all the answers

What is the primary function of Myosin I in living organisms?

<p>Facilitating membrane-membrane interactions (C)</p> Signup and view all the answers

Which Myosin class is specifically involved in organelle transport and found in all brain neurons?

<p>Myosin V (A)</p> Signup and view all the answers

What syndrome is associated with mutations in Myosin V?

<p>Elejalde syndrome (A)</p> Signup and view all the answers

Which amino acid residues are rich in the tail section of Myosin I?

<p>Basic amino acids (C)</p> Signup and view all the answers

What structural feature is unique to Myosin VI compared to other myosin classes?

<p>An extended neck region with calmodulin binding (B)</p> Signup and view all the answers

What is a characteristic symptom of Elejalde syndrome?

<p>Severe central nervous system dysfunction (A)</p> Signup and view all the answers

What region of Myosin I is important for binding to actin?

<p>The GPA domain (B)</p> Signup and view all the answers

How many classes of myosin have been identified in the human genome?

<p>18 (A)</p> Signup and view all the answers

Flashcards

Kinesins

Microtubule-based molecular motors that transport cellular cargo.

Function of Kinesins

They move vesicles, organelles, and chromosome portions within cells.

Dynein

Molecular motors that move in the opposite direction to kinesins and are involved in cilia and flagella movement.

Axonemal Dynein

A type of dynein that facilitates movement of cilia and flagella.

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Cytoplasmic Dynein

Dynein that organizes and distributes cytoplasmic structures within the cell.

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Myosins

Biological machines that facilitate movement in living organisms.

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Myosin Classes

Eighteen classes of myosin are found in the human genome, including Class II for muscle myosins.

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Myosin I

A low-molecular-mass motor protein that interacts with cell membranes and aids in membrane transport.

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GPA Domain

A tail section in Myosin I rich in glycine, proline, and alanine that helps bind to actin.

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Myosin V

A myosin class involved in transport of organelles, found in neurons and needed for melanosome transport.

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Elejalde Syndrome

A condition marked by silvery hair and central nervous system dysfunction due to defective melanin transport.

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Myosin VI

A myosin expressed in most cells, extended neck region with a binding site for calmodulin.

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Calmodulin Binding Region

Part of Myosin VI's structure that interacts with calmodulin for calcium signaling.

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Study Notes

Myosins and Molecular Motors

  • Myosins are biological machines driving movement in living organisms.

Myosin Classes

  • Eighteen myosin classes are identified in the human genome.
  • Myosin I-XVIII;
  • Skeletal, cardiac, and smooth muscle myosins fall under Class II.

Myosin I

  • A low molecular weight motor protein associated with cell membranes.
  • Contains a tail rich in basic amino acids that can bind to anionic phospholipids.
  • Contains a glycine, proline, alanine (GPA) domain facilitating actin binding.
  • Involved in membrane-membrane interactions and functions in the brush borders of small intestines.
  • Possibly involved in transporting Golgi-derived vesicles.

Myosin V

  • Involved in organelle transport (synaptic vesicles, melanosomes, vacuoles, mRNA).
  • Found in all brain neurons; required for melanosome transport.
  • Mutations linked to neurological disorders and depigmentation, especially hair.

Elejalde Syndrome

  • Characterized by silvery hair and CNS dysfunction.
  • Large melanin granules unevenly distributed in hair shaft.
  • Abnormal melanocytes and melanosomes might be present in fibroblasts.
  • Suggests defective mechanisms for melanin movement and distribution.

Myosin VI

  • Expressed in most cells and tissues.
  • Extended neck region with one calmodulin (IQ motif) binding region per head.
  • A dimeric molecule with a coiled tail and two globular ends (one per monomer).
  • Defects in the gene cause hearing problems due to hair movement defects in the inner ear.

Kinesins

  • Microtubule-based molecular motors.
  • Do not form filaments like some myosins.
  • Generate motion by conformational changes upon ATP binding and hydrolysis.
  • Similar mechanism to myosin actin-based motors.
  • Structure includes two heavy chains and two light chains.
  • Includes microtubule and ATP binding sites in the head and cargo-binding sites in the tail.

Kinesin 1

  • Na/K-ATPase containing vesicle transport via kinesin 1 on microtubules (KLC2, KHC).

Dynein

  • Axonemal dynein affecting flagella and cilia movement.
  • Cytoplasmic dynein affecting cytoplasmic structure distribution and organization.
  • Structure includes a spherical globular head, stalk, and light chains attached to a cargo. Movement on microtubule.

Molecular Motor Comparison

  • Comparison diagrams illustrating the modes of action for dynein, myosin, and kinesin heavy chain movement along their respective tracks (microtubules, actin filaments).

Additional Information

  • T. Devlin's Textbook of Biochemistry (pp. 979-981) provides further details.

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