Dynamin is membrane-active: lipid insertion is induced by phosphoinositides and phosphatidic acid.

Abstract:

:Dynamin is a large GTPase involved in the regulation of membrane constriction and fission during receptor-mediated endocytosis. Dynamin contains a pleckstrin-homology domain which is essential for endocytosis and which binds to anionic phospholipids. Here, we show for the first time that dynamin is a membrane-active molecule capable of penetrating into the acyl chain region of membrane lipids. Lipid penetration is strongly stimulated by phosphatidic acid (PA), phosphatidylinositol 4-phosphate, and phosphatidylinositol 4, 5-bisphosphate. Though binding is more efficient in the presence of the phosphoinositides, a much larger part of the dynamin molecule penetrates into PA-containing mixed-lipid systems. Thus, local lipid metabolism will dramatically influence dynamin-lipid interactions, and dynamin-lipid interactions are likely to play an important role in dynamin-dependent endocytosis. Our data suggest that dynamin is directly involved in membrane destabilization, a prerequisite to membrane fission.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Burger KN,Demel RA,Schmid SL,de Kruijff B

doi

10.1021/bi000971r

subject

Has Abstract

pub_date

2000-10-10 00:00:00

pages

12485-93

issue

40

eissn

0006-2960

issn

1520-4995

pii

bi000971r

journal_volume

39

pub_type

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