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Updated: Dec 25, 2025

Measuring In Vitro ATPase Activity for Enzymatic Characterization
Published on: August 23, 2016
Cellular functions and intrinsic attributes of the ATP-binding Eps15 homology domain-containing proteins
Soumya Bhattacharyya1, Thomas J Pucadyil1
1Department of Biology, Indian Institute of Science Education and Research, Pune, India.
Abstract:
Several cellular processes rely on a cohort of dedicated proteins that manage tubulation, fission, and fusion of membranes. A notably large number of them belong to the dynamin superfamily of proteins. Among them is the evolutionarily conserved group of ATP-binding Eps15-homology domain-containing proteins (EHDs). In the two decades since their discovery, EHDs have been linked to a range of cellular processes that require remodeling or maintenance of specific membrane shapes such as during endocytic recycling, caveolar biogenesis, ciliogenesis, formation of T-tubules in skeletal muscles, and membrane resealing after rupture. Recent work has shed light on their structure and the unique attributes they possess in linking ATP hydrolysis to membrane remodeling. This review summarizes some of these recent developments and reconciles intrinsic protein functions to their cellular roles.
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