Regulatory mechanisms of dynamin-dependent endocytosis

Research output: Contribution to journalArticle

61 Citations (Scopus)

Abstract

Extensive studies on endocytosis in the last decade have resulted in identification of several key molecules that function in clathrin- and dynamin-dependent endocytosis. Most endocytic molecules contain multiple binding motifs that mediate protein-protein or protein-lipid interactions, which must be modulated spatially and temporally during endocytosis. Regulation of these interactions is the molecular basis of regulatory mechanisms involved in endocytosis. This review first describes current models of the mechanism of dynamin-dependent fission, then introduces several mechanisms that modulate dynamin GTPase activity and dynamin-dependeat vesicle formation. Such mechanisms include regulation by inositol phospholipids, especially phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2], and their metabolism. It concludes by describing the regulation of dynamin 1 by its binding partner, amphiphysin 1, and regulation by cyclin-dependent kinase 5 (Cdk5)-dependent phosphorylation of dynamin 1 and amphiphysin 1. These mechanisms help endocytic molecules to function properly, and cooperatively regulate dynamin-dependent endocytosis.

Original languageEnglish
Pages (from-to)243-247
Number of pages5
JournalJournal of Biochemistry
Volume137
Issue number3
DOIs
Publication statusPublished - Mar 2005

Fingerprint

Dynamins
Endocytosis
Dynamin I
Phosphatidylinositols
Molecules
Cyclin-Dependent Kinase 5
Phosphatidylinositol 4,5-Diphosphate
Clathrin
Amino Acid Motifs
Phosphorylation
Proteins
GTP Phosphohydrolases
Metabolism
Lipids

Keywords

  • Amphiphysin
  • Clathrin
  • Cyclin-dependent kinase 5
  • Dynamin
  • Endocytosis

ASJC Scopus subject areas

  • Biochemistry

Cite this

Regulatory mechanisms of dynamin-dependent endocytosis. / Takei, Kohji; Yoshida, Yumi; Yamada, Hiroshi.

In: Journal of Biochemistry, Vol. 137, No. 3, 03.2005, p. 243-247.

Research output: Contribution to journalArticle

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