Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/4556
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dc.contributor.authorBHATTACHARYYA, SOUMYAen_US
dc.contributor.authorPUCADYIL, THOMAS J.en_US
dc.date.accessioned2020-04-24T09:07:11Z
dc.date.available2020-04-24T09:07:11Z
dc.date.issued2020-06en_US
dc.identifier.citationProtein Science, 29(6), 1321-1330.en_US
dc.identifier.issn1469-896Xen_US
dc.identifier.urihttp://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/4556
dc.identifier.urihttps://doi.org/10.1002/pro.3860en_US
dc.description.abstractSeveral 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.en_US
dc.language.isoenen_US
dc.publisherWileyen_US
dc.subjectATPasesen_US
dc.subjectCaveolaeen_US
dc.subjectCiliaen_US
dc.subjectDynamin superfamilyen_US
dc.subjectEndocytic recyclingen_US
dc.subjectEps15‐homology domainen_US
dc.subjectMembrane fissionen_US
dc.subjectMembrane tubulationen_US
dc.subjectT‐tubulesen_US
dc.subjectTOC-APR-2020en_US
dc.subject2020en_US
dc.subject2020-APR-WEEK4en_US
dc.titleCellular functions and intrinsic attributes of the ATP‐binding Eps15 homology domain‐containing proteinsen_US
dc.typeArticleen_US
dc.contributor.departmentDept. of Biologyen_US
dc.identifier.sourcetitleProtein Scienceen_US
dc.publication.originofpublisherForeignen_US
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