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Proteomic analysis of the cellular targets of a divalent synthetic SH3 domain ligand

ABSTRACT: Comparative LC/MS/MS analysis of pull-down material from an adult rat brain lysate between streptavidin-coated magnetic beads functionalized with either a biotinylated divalent peptide derived from the dynamin proline-rich domain or biotin

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Rattus Norvegicus (rat)

SUBMITTER: Stephane Claverol

LAB HEAD: Marc Bonneu

PROVIDER: PXD015292 | Pride | 2019-11-12

REPOSITORIES: Pride

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Functional recruitment of dynamin requires multimeric interactions for efficient endocytosis.

Rosendale Morgane M Van Thi Nhu Ngoc TNN Grillo-Bosch Dolors D Sposini Silvia S Claverie Léa L Gauthereau Isabel I Claverol Stéphane S Choquet Daniel D Sainlos Matthieu M Perrais David D

Nature communications 20191001 1

During clathrin mediated endocytosis (CME), the concerted action of dynamin and its interacting partners drives membrane scission. Essential interactions occur between the proline/arginine-rich domain of dynamin (dynPRD) and the Src-homology domain 3 (SH3) of various proteins including amphiphysins. Here we show that multiple SH3 domains must bind simultaneously to dynPRD through three adjacent motifs for dynamin's efficient recruitment and function. First, we show that mutant dynamins modified ...[more]

PMID: 31575863

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Critical role of Aquaporin-1 and telocytes in infantile hemangioma response to propranolol beta-blockade

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