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dc.contributor.authorCahill, Michael A
dc.contributor.authorJazayeri, Jalal A
dc.contributor.authorKovacevic, Zaklina
dc.contributor.authorRichardson, Des R
dc.date.accessioned2021-04-30T01:07:56Z
dc.date.available2021-04-30T01:07:56Z
dc.date.issued2016
dc.identifier.issn1949-2553
dc.identifier.doi10.18632/oncotarget.10691
dc.identifier.urihttp://hdl.handle.net/10072/404049
dc.description.abstractProgesterone receptor membrane component 1 (PGRMC1) is a multifunctional protein implicated in multiple pathologies, including cancer and Alzheimer's disease. The recently published structure of PGRMC1 revealed heme-mediated dimerization that directed the PGRMC1-dependent cytochrome P450-mediated detoxification of doxorubicin. We describe here how the PGRMC1 structure also enables important new insights into the possible regulation of PGRMC1 function by phosphorylation. Predicted regulatory interaction sites for SH2- and SH3-domain proteins are in nonstructured regions that could be available to cytoplasmic enzymes. Further to the published interpretation, we suggest that phosphorylation of PGRMC1 at position Y113 may promote the attested membrane trafficking function of PGRMC1. To stimulate further experimentation, we also discuss that heme-mediated dimerization of PGRMC1 and membrane trafficking may be mutually exclusive functions. These roles could potentially be reciprocally regulated by phosphorylation/dephosphorylation at Y113. It follows that the phosphorylation status of PGRMC1 should be further explored in order to better understand many of its proposed biological functions.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherImpact Journals, LLC
dc.relation.ispartofpagefrom50822
dc.relation.ispartofpageto50827
dc.relation.ispartofissue32
dc.relation.ispartofjournalOncotarget
dc.relation.ispartofvolume7
dc.subject.fieldofresearchOncology and carcinogenesis
dc.subject.fieldofresearchcode3211
dc.subject.keywordsScience & Technology
dc.subject.keywordsLife Sciences & Biomedicine
dc.subject.keywordsCell Biology
dc.subject.keywordssignaling
dc.titlePGRMC1 regulation by phosphorylation: potential new insights in controlling biological activity
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationCahill, MA; Jazayeri, JA; Kovacevic, Z; Richardson, DR, PGRMC1 regulation by phosphorylation: potential new insights in controlling biological activity, Oncotarget, 2016, 7 (32), pp. 50822-50827
dcterms.dateAccepted2016-06-20
dcterms.licensehttp://creativecommons.org/licenses/by/3.0/
dc.date.updated2021-04-30T01:04:08Z
dc.description.versionVersion of Record (VoR)
gro.rights.copyright© The Author(s) 2016. This is an Open Access article distributed under the terms of the Creative Commons Attribution 3.0 Unported (CC BY 3.0) License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
gro.hasfulltextFull Text
gro.griffith.authorRichardson, Des R.


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