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001-es BibID:	BIBFORM036713
Első szerző:	Bögel Gábor
Cím:	Frank-ter Haar syndrome protein Tks4 regulates EGF-dependent cell migration / Gábor Böge, Annamária Gujdár, Miklós Geiszt, Árpád Lányi, Anna Fekete, Szabolcs Sipeki, Julian Downward, László Buday
Dátum:	2012
ISSN:	0021-9258
Megjegyzések:	Mutations in the SH3PXD2B gene coding for the Tks4 protein are responsible for the autosomal-recessive Frank-ter Haar syndrome. Tks4, a substrate of Src tyrosine kinase is implicated in the regulation of podosome formation. Here, we report a novel role for Tks4 in the EGF signalling pathway. In EGF-treated cells, Tks4 is tyrosine phosphorylated and associated with the activated EGF receptor. This association is not direct but requires the presence of Src tyrosine kinase. In addition, treatment of cells with LY294002, an inhibitor of PI 3-kinase, or mutations of the PX domain reduces tyrosine phosphorylation and membrane translocation of Tks4. Furthermore, a PX domain mutant (R43W) Tks4 carrying a reported point mutation in a Frank-ter Haar syndrome patient showed aberrant intracellular expression and reduced phosphoinositide binding. Finally, silencing of Tks4 was shown to markedly inhibit HeLa cell migration in a Boyden chamber assay in response to EGF or serum. Our results therefore reveal a new function for Tks4 in the regulation of growth factor-dependent cell migration.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban EGF receptor Tks4 cell migration Frank-ter Haar syndrome PX domain Molekuláris Medicina
Megjelenés:	Journal Of Biological Chemistry. - 287 : 37 (2012), p. 31321-31329. -
További szerzők:	Gujdár Annamária Geiszt Miklós Lányi Árpád (1962-) (biológus, immunológus) Fekete Anna Sipeki Szabolcs Downward, Julian Buday László
Pályázati támogatás:	TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP A HOFI/SH3PXD2B aktin citoszkeletont szabályozó új adaptor fehérje funkcionális vizsgálata
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001-es BibID:	BIBFORM065580
Első szerző:	Morra, Massimo
Cím:	Characterization of SH2D1A Missense Mutations Identified in X-linked Lymphoproliferative Disease Patients / Massimo Morra, Maria Simarro-Grande, Margarita Martin, Alice Siau-In Chen, Arpad Lanyi, Olin Silander, Silvia Calpe, Jack Davis, Tony Pawson, Michael J. Eck, Janos Sumegi, Pablo Engel, Shun-Cheng Li, Cox Terhorsta
Dátum:	2001
ISSN:	0021-9258 1083-351X
Megjegyzések:	X-linked lymphoproliferative disease (XLP) is a primary immunodeficiency characterized by extreme susceptibility to Epstein-Barr virus. The XLP disease gene product SH2D1A (SAP) interacts via its SH2 domain with a motif (TIYXXV) present in the cytoplasmic tail of the cell-surface receptors CD150/SLAM, CD84, CD229/Ly-9, and CD244/2B4. Characteristically, the SH2D1A three-pronged interaction with Tyr(281) of CD150 can occur in absence of phosphorylation. Here we analyze the effect of SH2D1A protein missense mutations identified in 10 XLP families. Two sets of mutants were found: (i) mutants with a marked decreased protein half-life (e.g. Y7C, S28R, Q99P, P101L, V102G, and X129R) and (ii) mutants with structural changes that differently affect the interaction with the four receptors. In the second group, mutations that disrupt the interaction between the SH2D1A hydrophobic cleft and Val +3 of its binding motif (e.g. T68I) and mutations that interfere with the SH2D1A phosphotyrosine-binding pocket (e.g. C42W) abrogated SH2D1A binding to all four receptors. Surprisingly, a mutation in SH2D1A able to interfere with Thr -2 of the CD150 binding motif (mutant T53I) severely impaired non-phosphotyrosine interactions while preserving unaffected the binding of SH2D1A to phosphorylated CD150. Mutant T53I, however, did not bind to CD229 and CD224, suggesting that SH2D1A controls several critical signaling pathways in T and natural killer cells. Because no correlation is present between identified types of mutations and XLP patient clinical presentation, additional unidentified genetic or environmental factors must play a strong role in XLP disease manifestations.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal Of Biological Chemistry 276 : 39 (2001), p. 36809-36816. -
További szerzők:	Simarro-Grande, Maria Martin, Margarita Chen, Alice Siau-In Lányi Árpád (1962-) (biológus, immunológus) Silander, Olin Calpe, Silvia Davis, Jack Pawson, Tony Eck, Michael J. Sümegi János Engel, Pablo Li, Shun-Cheng Terhorst, Cox
Pályázati támogatás:	PO1-AI-35714 Egyéb
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