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Dynamin and its partners: a progress report

S L Schmid¹, M A McNiven, P De Camilli

¹Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA.

Current Opinion in Cell Biology

|August 28, 1998

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Dynamin, a GTPase, is crucial for clathrin-mediated endocytosis. Recent research reveals its expanded roles in intracellular trafficking, domain functions, and interactions with partner proteins.

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Dynamin's established role in clathrin-mediated endocytosis.
Emerging evidence suggests dynamin participates in diverse intracellular trafficking pathways.

Purpose of the Study:

To review recent findings on dynamin and related GTPases in intracellular trafficking.
To summarize dynamin's domain structure and functional significance.
To describe dynamin-interacting partners and their roles in endocytosis.

Main Methods:

Literature review of studies published in the last two years.
Analysis of domain structure and function of dynamin.
Synthesis of information on dynamin-binding partners.

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Main Results:

Dynamin and related GTPases are implicated in multiple intracellular trafficking events beyond endocytosis.
Detailed understanding of dynamin's multidomain structure and its functional implications.
Identification and functional characterization of key dynamin partners in endocytic pathways.

Conclusions:

Dynamin's functions extend beyond clathrin-mediated endocytosis.
Understanding dynamin's structure-function relationships and its interaction network is vital for elucidating its diverse roles in cellular trafficking.