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Dynamin: a microtubule-associated GTP-binding protein.
R A Obar1, H S Shpetner, R B Vallee
1Cell Biology Group, Worcester Foundation for Experimental Biology, Shrewsbury, MA 01545.
Journal of Cell Science. Supplement
|January 1, 1991
Summary
Dynamin, a novel GTP-binding protein, was identified as a microtubule-associated protein in brain tissue. This discovery reveals a new class of GTP-utilizing proteins with diverse cellular functions.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Microtubule-associated proteins (MAPs) are crucial for cellular functions.
- Kinesin and cytoplasmic dynein are known nucleotide-sensitive MAPs.
- The role of other nucleotide-sensitive proteins in microtubule dynamics was unclear.
Purpose of the Study:
- To identify novel nucleotide-sensitive microtubule-associated proteins in brain tissue.
- To characterize the molecular and biochemical properties of the identified protein.
- To explore the functional and evolutionary significance of this new protein class.
Main Methods:
- Protein identification in brain tissue.
- Molecular cloning and sequence analysis.
- GTP-binding assays and biochemical characterization.
Main Results:
- Dynamin was identified as a third nucleotide-sensitive MAP in brain.
- Dynamin possesses three consensus elements characteristic of GTP-binding proteins.
- Dynamin is homologous to yeast VPS1 and Mx proteins, suggesting diverse functions.
Conclusions:
- Dynamin represents a novel class of GTP-utilizing proteins.
- This protein family has diverse roles in cellular processes.
- Further research into dynamin's function is warranted.