A Screen for Membrane Fission Catalysts Identifies the ATPase EHD1 | Zendy

Sukrut C. Kamerkar | Zendy; Krishnendu Roy | Zendy; Soumya Bhattacharyya | Zendy; Thomas J. Pucadyil | Zendy

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A Screen for Membrane Fission Catalysts Identifies the ATPase EHD1

Author(s) -

Sukrut C. Kamerkar,

Krishnendu Roy,

Soumya Bhattacharyya,

Thomas J. Pucadyil

Publication year - 2018

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/acs.biochem.8b00925

Subject(s) - fission , gtpase , membrane , chemistry , biogenesis , gtp' , organelle , dynamin , cytosol , synaptic vesicle recycling , atpase , microbiology and biotechnology , biophysics , biochemistry , endocytosis , vesicle , biology , synaptic vesicle , cell , enzyme , physics , gene , quantum mechanics , neutron

Membrane fission manifests during cell division, synaptic transmission, vesicular transport, and organelle biogenesis, yet identifying proteins that catalyze fission remains a challenge. Using a facile and robust assay system of supported membrane tubes in a microscopic screen that directly monitors membrane tube scission, we detect robust GTP- and ATP-dependent as well as nucleotide-independent fission activity in the brain cytosol. Using previously established interacting partner proteins as bait for pulldowns, we attribute the GTP-dependent fission activity to dynamin. Biochemical fractionation followed by mass spectrometric analyses identifies the Eps15-homology domain-containing protein1 (EHD1) as a novel ATP-dependent membrane fission catalyst. Together, our approach establishes an experimental workflow for the discovery of novel membrane fission catalysts.

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