beta-Arrestin Promotes Wnt-induced Low Density Lipoprotein Receptor-related Protein 6 (Lrp6) Phosphorylation via Increased Membrane Recruitment of Amer1 Protein

0427976 - BFÚ 2015 RIV US eng J - Článek v odborném periodiku
Kříž, Vitězslav - Pospíchalová, V. - Mašek, Jan - Kilander, M.B.C. - Slavík, J. - Tanneberger, K. - Schulte, G. - Machala, M. - Kozubík, Alois - Behrens, J. - Bryja, Vítězslav
beta-Arrestin Promotes Wnt-induced Low Density Lipoprotein Receptor-related Protein 6 (Lrp6) Phosphorylation via Increased Membrane Recruitment of Amer1 Protein.
Journal of Biological Chemistry. Roč. 289, č. 2 (2014), s. 1128-1141. ISSN 0021-9258. E-ISSN 1083-351X
Grant CEP: GA ČR(CZ) GA204/09/0498; GA ČR(CZ) GA13-32990S
Grant ostatní: GA ČR(CZ) GC204/09/J030
Institucionální podpora: RVO:68081707 ; RVO:68378050
Klíčová slova: CONVERGENT EXTENSION MOVEMENTS * SIGNALING PATHWAYS * IN-VIVO
Kód oboru RIV: BO - Biofyzika; EB - Genetika a molekulární biologie (UMG-J)
Impakt faktor: 4.573, rok: 2014

beta-Arrestin is a scaffold protein that regulates signal transduction by seven transmembrane-spanning receptors. Among other functions it is also critically required for Wnt/beta-catenin signal transduction. In the present study we provide for the first time a mechanistic basis for the beta-arrestin function in Wnt/beta-catenin signaling. We demonstrate that beta-arrestin is required for efficient Wnt3a-induced Lrp6 phosphorylation, a key event in downstream signaling. beta-Arrestin regulates Lrp6 phosphorylation via a novel interaction with phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P-2)-binding protein Amer1/WTX/Fam123b. Amer1 has been shown very recently to bridge Wnt-induced and Dishevelled-associated PtdIns(4,5)P-2 production to the phosphorylation of Lrp6. Using fluorescence recovery after photobleaching we show here that beta-arrestin is required for the Wnt3a-induced Amer1 membrane dynamics and downstream signaling.
Trvalý link: http://hdl.handle.net/11104/0233415