FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2216263487> ?p ?o ?g. }

• W2216263487 abstract "In the due course of the formation of apical-basal polarity the transmembrane protein Crumbs (Crb) and its intracellular adaptor protein Pals1 (Protein associated with Lin seven 1, Stardust, Sdt in Drosophila) have been found to play key roles in the establishment and maintenance of cell polarity in various types of tissues. Research in Drosophila revealed that PATJ (Pals1 associated tight junction protein) which have been reported to be a part of the trimeric complex with Crb-Sdt localizes at the apical cell-cell contacts and plays roles in the formation of the tight junction and cell migration in mammalian cells. However it is not yet fully understood how PATJ has been localized to the apical cell junctions and its role in the regulation and maintenance of cell polarity.In this vivid study in elucidating functional significance of PATJ, a systematic structural-functional analysis have been carried out with deletion constructs tagged with green fluorescent protein (GFP) in transgenic flies to elucidate the roles of each conserved domain of the protein. In our study we found that the N-terminally located L27 domain along with a redundancy of the PDZ domains is required for proper functionality of the protein. Further we also found that PATJ attaches to both Baz-Sdt and Crb-Sdt complexes for its proper functionality. On our way to decipher how PATJ shuffles between these two complexes, we reveal the role of PAR6 in stabilizing Crb-Sdt complex via selective inhibition of Sdt degradation by ubiquitin mediated proteosomal pathway. Additionally we have found that PATJ is not per se crucial for the establishment or maintenance of apical-basal polarity, but rather regulates Myosin dynamics. PATJ directly binds to the Myosin Binding Subunit of Myosin Phosphatase and decreases Myosin dephosphorylation, resulting in activated Myosin dynamics. Thereby PATJ supports the stability of the Zonula Adherens. Notably, weakening of Adherens Junction (AJ) in a PATJ-mutant epithelium leads first to a loss of Myosin from the AJ, subsequently to a disassembly of the AJ and finally to a loss of apical-basal polarity and disruption of the tissue.%%%%Wahrend der Entwicklung einer apikal-basalen Zellpolaritat hat sich gezeigt, dass das Trans-membranprotein Crumbs (Crb) und dessen intrazellulares Adapterprotein Pals1 (Protein associated with Lin seven 1, Stardust, Sdt in Drosophila) eine Schlusselrolle in der Etablierung und Aufrechterhaltung dieser Polaritat einnehmen. In Drosophila konnte gezeigt werden, dass PATJ (Pals1 associated tight junction protein) als Teil eines trimeren Komplexes zusammen mit Crb-Sdt an den apikalen Zell-Zell Kontakten lokalisiert und zur Formierung der Tight Junctions und der Zellmigration in Saugetieren beitragt. Allerdings sind weder der Mechanismus durch den PATJ an die apikalen Zell-Zell Kontakte lokalisiert wird noch die Rolle in der Regulation der Zellpolaritat von PATJ vollig verstanden. In dieser Studie wurde die funktionelle Bedeutung von PATJ untersucht. Dazu wurde eine systematische…" @default.
• W2216263487 created "2016-06-24" @default.
• W2216263487 creator A5060354163 @default.
• W2216263487 date "2015-12-17" @default.
• W2216263487 modified "2023-09-23" @default.
• W2216263487 title "The role of PATJ in the development of Drosophila melanogaster" @default.
• W2216263487 hasPublicationYear "2015" @default.
• W2216263487 type Work @default.
• W2216263487 sameAs 2216263487 @default.
• W2216263487 citedByCount "0" @default.
• W2216263487 crossrefType "dissertation" @default.
• W2216263487 hasAuthorship W2216263487A5060354163 @default.
• W2216263487 hasConcept C104317684 @default.
• W2216263487 hasConcept C1491633281 @default.
• W2216263487 hasConcept C154428179 @default.
• W2216263487 hasConcept C170493617 @default.
• W2216263487 hasConcept C183786373 @default.
• W2216263487 hasConcept C24530287 @default.
• W2216263487 hasConcept C2777361361 @default.
• W2216263487 hasConcept C2780104201 @default.
• W2216263487 hasConcept C49353375 @default.
• W2216263487 hasConcept C55493867 @default.
• W2216263487 hasConcept C62478195 @default.
• W2216263487 hasConcept C86803240 @default.
• W2216263487 hasConcept C95444343 @default.
• W2216263487 hasConceptScore W2216263487C104317684 @default.
• W2216263487 hasConceptScore W2216263487C1491633281 @default.
• W2216263487 hasConceptScore W2216263487C154428179 @default.
• W2216263487 hasConceptScore W2216263487C170493617 @default.
• W2216263487 hasConceptScore W2216263487C183786373 @default.
• W2216263487 hasConceptScore W2216263487C24530287 @default.
• W2216263487 hasConceptScore W2216263487C2777361361 @default.
• W2216263487 hasConceptScore W2216263487C2780104201 @default.
• W2216263487 hasConceptScore W2216263487C49353375 @default.
• W2216263487 hasConceptScore W2216263487C55493867 @default.
• W2216263487 hasConceptScore W2216263487C62478195 @default.
• W2216263487 hasConceptScore W2216263487C86803240 @default.
• W2216263487 hasConceptScore W2216263487C95444343 @default.
• W2216263487 hasLocation W22162634871 @default.
• W2216263487 hasOpenAccess W2216263487 @default.
• W2216263487 hasPrimaryLocation W22162634871 @default.
• W2216263487 hasRelatedWork W1978345539 @default.
• W2216263487 hasRelatedWork W2008881930 @default.
• W2216263487 hasRelatedWork W2009671571 @default.
• W2216263487 hasRelatedWork W2010994824 @default.
• W2216263487 hasRelatedWork W2023784682 @default.
• W2216263487 hasRelatedWork W2034696312 @default.
• W2216263487 hasRelatedWork W2036648103 @default.
• W2216263487 hasRelatedWork W2048529602 @default.
• W2216263487 hasRelatedWork W2052478337 @default.
• W2216263487 hasRelatedWork W2057226949 @default.
• W2216263487 hasRelatedWork W2074618332 @default.
• W2216263487 hasRelatedWork W2091470454 @default.
• W2216263487 hasRelatedWork W2096823291 @default.
• W2216263487 hasRelatedWork W2099231076 @default.
• W2216263487 hasRelatedWork W2125031377 @default.
• W2216263487 hasRelatedWork W2133862855 @default.
• W2216263487 hasRelatedWork W2168436318 @default.
• W2216263487 hasRelatedWork W2736607612 @default.
• W2216263487 hasRelatedWork W3190283531 @default.
• W2216263487 hasRelatedWork W153893742 @default.
• W2216263487 isParatext "false" @default.
• W2216263487 isRetracted "false" @default.
• W2216263487 magId "2216263487" @default.
• W2216263487 workType "dissertation" @default.