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Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis

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  • Sanja Sever

    (The Scripps Research Institute)

  • Amy B. Muhlberg

    (The Scripps Research Institute)

  • Sandra L. Schmid

    (The Scripps Research Institute)

Abstract

Dynamin is a GTP-hydrolysing protein that is an essential participant in clathrin-mediated endocytosis by cells. It self-assembles into ‘collars’ in vitro which also form in vivo at the necks of invaginated coated pits. This self-assembly stimulates dynamin's GTPase activity and it has been proposed that dynamin hydrolyses GTP in order to generate the force needed to sever vesicles from the plasma membrane. A mechanism is now described in which self-assembly of dynamin is coordinated by a domain of dynamin with a GTPase-activating function. Unexpectedly, when dynamin mutants defective in self-assembly-stimulated GTPase activity are overexpressed, receptor-mediated endocytosis is accelerated. The results indicate that dynamin, like other members of the GTPase superfamily, functions as a molecular regulator in receptor-mediated endocytosis, rather than as a force-generating GTPase.

Suggested Citation

  • Sanja Sever & Amy B. Muhlberg & Sandra L. Schmid, 1999. "Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis," Nature, Nature, vol. 398(6727), pages 481-486, April.
    • Handle: RePEc:nat:nature:v:398:y:1999:i:6727:d:10.1038_19024
    DOI: 10.1038/19024
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    Cited by:

    1. Katherine Bonnycastle & Katharine L. Dobson & Eva-Maria Blumrich & Akshada Gajbhiye & Elizabeth C. Davenport & Marie Pronot & Moritz Steinruecke & Matthias Trost & Alfredo Gonzalez-Sulser & Michael A., 2023. "Reversal of cell, circuit and seizure phenotypes in a mouse model of DNM1 epileptic encephalopathy," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    2. Isabel Pérez-Jover & Kristy Rochon & Di Hu & Mukesh Mahajan & Pooja Madan Mohan & Isaac Santos-Pérez & Julene Ormaetxea Gisasola & Juan Manuel Martinez Galvez & Jon Agirre & Xin Qi & Jason A. Mears & , 2024. "Allosteric control of dynamin-related protein 1 through a disordered C-terminal Short Linear Motif," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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