The PH Domain and C-Terminal polyD Motif of Phafin2 Exhibit a Unique Concurrence in Animals

dc.contributor.authorHasan, Mahmudulen
dc.contributor.authorCapelluto, Daniel G. S.en
dc.date.accessioned2022-07-08T12:05:35Zen
dc.date.available2022-07-08T12:05:35Zen
dc.date.issued2022-07-07en
dc.date.updated2022-07-08T11:55:16Zen
dc.description.abstractPhafin2, a member of the Phafin family of proteins, contributes to a plethora of cellular activities including autophagy, endosomal cargo transportation, and macropinocytosis. The PH and FYVE domains of Phafin2 play key roles in membrane binding, whereas the C-terminal poly aspartic acid (polyD) motif specifically autoinhibits the PH domain binding to the membrane phosphatidylinositol 3-phosphate (PtdIns3P). Since the Phafin2 FYVE domain also binds PtdIns3P, the role of the polyD motif remains unclear. In this study, bioinformatics tools and resources were employed to determine the concurrence of the PH-FYVE module with the polyD motif among Phafin2 and PH-, FYVE-, or polyD-containing proteins from bacteria to humans. FYVE was found to be an ancient domain of Phafin2 and is related to proteins that are present in both prokaryotes and eukaryotes. Interestingly, the polyD motif only evolved in Phafin2 and PH- or both PH-FYVE-containing proteins in animals. PolyD motifs are absent in PH domain-free FYVE-containing proteins, which usually display cellular trafficking or autophagic functions. Moreover, the prediction of the Phafin2-interacting network indicates that Phafin2 primarily cross-talks with proteins involved in autophagy, protein trafficking, and neuronal function. Taken together, the concurrence of the polyD motif with the PH domain may be associated with complex cellular functions that evolved specifically in animals.en
dc.description.versionPublished versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.citationHasan, M.; Capelluto, D.G.S. The PH Domain and C-Terminal polyD Motif of Phafin2 Exhibit a Unique Concurrence in Animals. Membranes 2022, 12, 696.en
dc.identifier.doihttps://doi.org/10.3390/membranes12070696en
dc.identifier.urihttp://hdl.handle.net/10919/111178en
dc.language.isoenen
dc.publisherMDPIen
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectPhafin2en
dc.subjectPH domainen
dc.subjectpolyD motifen
dc.subjectFYVE domainen
dc.subjectbioinformaticsen
dc.titleThe PH Domain and C-Terminal polyD Motif of Phafin2 Exhibit a Unique Concurrence in Animalsen
dc.title.serialMembranesen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten

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