The dynamin family of mechanoenzymes: Pinching in new places

Mark A. McNiven, Hong Cao, Kelly R. Pitts, Yisang Yoon

Research output: Contribution to journalReview article

301 Citations (Scopus)

Abstract

The large GTPase dynamin is a mechanoenzyme that mediates the liberation of nascent clathrin-coated pits from the plasma membrane during endocytosis. Recently, this enzyme has been demonstrated to comprise an extensive family of related proteins that have been implicated in a large variety of vesicle trafficking events during endocytosis, secretion and even maintenance of mitochondrial form. The potential contributions by the dynamin family to these diverse but related functions are discussed. Copyright (C) 2000 Elsevier Science Ltd.

Original languageEnglish (US)
Pages (from-to)115-120
Number of pages6
JournalTrends in Biochemical Sciences
Volume25
Issue number3
DOIs
StatePublished - Mar 1 2000
Externally publishedYes

Fingerprint

Dynamins
Endocytosis
Clathrin
GTP Phosphohydrolases
Cell membranes
Maintenance
Cell Membrane
Enzymes
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

The dynamin family of mechanoenzymes : Pinching in new places. / McNiven, Mark A.; Cao, Hong; Pitts, Kelly R.; Yoon, Yisang.

In: Trends in Biochemical Sciences, Vol. 25, No. 3, 01.03.2000, p. 115-120.

Research output: Contribution to journalReview article

McNiven, Mark A. ; Cao, Hong ; Pitts, Kelly R. ; Yoon, Yisang. / The dynamin family of mechanoenzymes : Pinching in new places. In: Trends in Biochemical Sciences. 2000 ; Vol. 25, No. 3. pp. 115-120.
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