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

K. N J Burger, R. A. Demel, S. L. Schmid, B. De Kruijff

Research output: Contribution to journalArticle

78 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)12485-12493
Number of pages9
JournalBiochemistry
Volume39
Issue number40
DOIs
StatePublished - Oct 10 2000

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Dynamin is membrane-active: Lipid insertion is induced by phosphoinositides and phosphatidic acid'. Together they form a unique fingerprint.

  • Cite this

    Burger, K. N. J., Demel, R. A., Schmid, S. L., & De Kruijff, B. (2000). Dynamin is membrane-active: Lipid insertion is induced by phosphoinositides and phosphatidic acid. Biochemistry, 39(40), 12485-12493. https://doi.org/10.1021/bi000971r