Regulation of the PI3K pathway through a p85a monomer-homodimer equilibrium

Handle URI:
http://hdl.handle.net/10754/623372
Title:
Regulation of the PI3K pathway through a p85a monomer-homodimer equilibrium
Authors:
Aljedani, Safia Salim Eid; Walkiewicz, Katarzyna Wiktoria; Besong, Tabot M.D. ( 0000-0002-3572-1428 ) ; Hameed, Umar Farook Shahul ( 0000-0002-0552-7149 ) ; Muhammad, Reyhan; Aroid, Stefan
Abstract:
The phosphatidylinositol-3-kinase a (PI3Ka) is heterodimeric enzyme that is composed of p85a regulatory subunit and a p110a catalytic subunit. PI3Ka plays a key role in cell survival, growth and differentation. Owing to its role as a key regulator, the PI3Ka pathway is the most frequently mutated pathway in human cancers, and is targeted by many viruses to insure their survival and successful reproduction. Previous studies have shown that the equilibrium of p85 monomers and dimers regulates the PI3K pathway, suggesting that interrupting this equilibrium could lead to disease development. Moreover, studies suggest that the p85a monomers and dimers have opposing effects on PI3Ka signaling as only the p85a dimers bind to the PTEN phosphatase, whereas p85a monomers bind to the catalytic p110 subunit. However, the mechanism for dimerisation is controversial, and it is unknown why PTEN or p110a bind only dimer or monomer. Therefore, we combine molecular biology, biophsical, computational and structural methods to investigate the suprosingly complex p85 dimerisation mechanism and its control by ligands. Results may inspire novel theraputic approaches.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Conference/Event name:
Winter Enrichment Program 2017 - Poster Competition
Issue Date:
8-Jan-2017
Type:
Poster
Appears in Collections:
Posters; Winter Enrichment Program 2017

Full metadata record

DC FieldValue Language
dc.contributor.authorAljedani, Safia Salim Eiden
dc.contributor.authorWalkiewicz, Katarzyna Wiktoriaen
dc.contributor.authorBesong, Tabot M.D.en
dc.contributor.authorHameed, Umar Farook Shahulen
dc.contributor.authorMuhammad, Reyhanen
dc.contributor.authorAroid, Stefanen
dc.date.accessioned2017-05-07T05:47:59Z-
dc.date.available2017-05-07T05:47:59Z-
dc.date.issued2017-01-08-
dc.identifier.urihttp://hdl.handle.net/10754/623372-
dc.description.abstractThe phosphatidylinositol-3-kinase a (PI3Ka) is heterodimeric enzyme that is composed of p85a regulatory subunit and a p110a catalytic subunit. PI3Ka plays a key role in cell survival, growth and differentation. Owing to its role as a key regulator, the PI3Ka pathway is the most frequently mutated pathway in human cancers, and is targeted by many viruses to insure their survival and successful reproduction. Previous studies have shown that the equilibrium of p85 monomers and dimers regulates the PI3K pathway, suggesting that interrupting this equilibrium could lead to disease development. Moreover, studies suggest that the p85a monomers and dimers have opposing effects on PI3Ka signaling as only the p85a dimers bind to the PTEN phosphatase, whereas p85a monomers bind to the catalytic p110 subunit. However, the mechanism for dimerisation is controversial, and it is unknown why PTEN or p110a bind only dimer or monomer. Therefore, we combine molecular biology, biophsical, computational and structural methods to investigate the suprosingly complex p85 dimerisation mechanism and its control by ligands. Results may inspire novel theraputic approaches.en
dc.titleRegulation of the PI3K pathway through a p85a monomer-homodimer equilibriumen
dc.typePosteren
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.conference.dateJanuary 8-21 2017en
dc.conference.nameWinter Enrichment Program 2017 - Poster Competitionen
dc.conference.locationKAUSTen
kaust.authorAljedani, Safia Salim Eiden
kaust.authorWalkiewicz, Katarzyna Wiktoriaen
kaust.authorBesong, Tabot M.D.en
kaust.authorHameed, Umar Farook Shahulen
kaust.authorMuhammad, Reyhanen
kaust.authorAroid, Stefanen
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