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Endocytosis: How dynamin sets vesicles PHree!

Bottomley, MJ; Lo Surdo, P; Driscoll, PC; (1999) Endocytosis: How dynamin sets vesicles PHree! Current Biology , 9 (8)

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Abstract

The dynamin GTPase is required for clathrin-dependent, receptor-mediated endocytosis. Exciting new studies have shown that dynamin's pleckstrin homology domain binds to phosphatidylinositol 4, 5- bisphosphate in vivo, thus localising dynamin directly at the plasma membrane and ultimately enabling vesiculation

Type:Article
Title:Endocytosis: How dynamin sets vesicles PHree!
Additional information:UI - 99244962 LA - Eng RN - EC 3.6.1.- (dynamin) RN - EC 3.6.1.-(GTP Phosphohydrolases) RN - 0 (platelet protein P47) RN - 0 (Blood Proteins) PT - JOURNAL ARTICLE PT - REVIEW PT - REVIEW, TUTORIAL DA - 19990601 IS - 0960-9822 SB - M CY - ENGLAND JC -B44 AA - Author EM - 199908
Keywords:Endocytosis, Proteins, blood, review, Binding Sites, Blood Proteins, chemistry, Cytoplasmic Granules, Dimerization, dynamin, GTP Phosphohydrolase, GTP Phosphohydrolases, Intracellular Membranes, metabolism, physiology, platelet protein P47, Receptor, homology, Phosphatidylinositols, plasma, Plasma membrane
UCL classification:UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of)

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