Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.advenzreg.2006.01.013 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Phosphoinositide 5-phosphatases SKIP and SHIP2 in ruffles, the endoplasmic reticulum and the nucleus: An update.
Adv Biol Regul
January 2020
IRIBHM, Campus Erasme, ULB Bâtiment C, 808 Route de Lennik, 1070, Bruxelles, Belgium. Electronic address:
Phosphoinositides (PIs) are phosphorylated derivatives of phosphatidylinositol. They act as signaling molecules linked to essential cellular mechanisms in eukaryotic cells, such as cytoskeleton organization, mitosis, polarity, migration or invasion. PIs are phosphorylated and dephosphorylated by a large number of PI kinases and PI phosphatases acting at the 5-, 4- and 3- position of the inositol ring.
View Article and Find Full Text PDFBAR Proteins PSTPIP1/2 Regulate Podosome Dynamics and the Resorption Activity of Osteoclasts.
PLoS One
May 2017
Biotechnology Center, Technische Universität Dresden, Tatzberg 47-51, 01307, Dresden, Germany.
Bone resorption in vertebrates relies on the ability of osteoclasts to assemble F-actin-rich podosomes that condense into podosomal belts, forming sealing zones. Sealing zones segregate bone-facing ruffled membranes from other membrane domains, and disassemble when osteoclasts migrate to new areas. How podosome/sealing zone dynamics is regulated remains unknown.
View Article and Find Full Text PDFCharacterization of VPS34-IN1, a selective inhibitor of Vps34, reveals that the phosphatidylinositol 3-phosphate-binding SGK3 protein kinase is a downstream target of class III phosphoinositide 3-kinase.
Biochem J
November 2014
*MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
The Vps34 (vacuolar protein sorting 34) class III PI3K (phosphoinositide 3-kinase) phosphorylates PtdIns (phosphatidylinositol) at endosomal membranes to generate PtdIns(3)P that regulates membrane trafficking processes via its ability to recruit a subset of proteins possessing PtdIns(3)P-binding PX (phox homology) and FYVE domains. In the present study, we describe a highly selective and potent inhibitor of Vps34, termed VPS34-IN1, that inhibits Vps34 with 25 nM IC50 in vitro, but does not significantly inhibit the activity of 340 protein kinases or 25 lipid kinases tested that include all isoforms of class I as well as class II PI3Ks. Administration of VPS34-IN1 to cells induces a rapid dose-dependent dispersal of a specific PtdIns(3)P-binding probe from endosome membranes, within 1 min, without affecting the ability of class I PI3K to regulate Akt.
View Article and Find Full Text PDFReversible Ser/Thr SHIP phosphorylation: a new paradigm in phosphoinositide signalling?: Targeting of SHIP1/2 phosphatases may be controlled by phosphorylation on Ser and Thr residues.
Bioessays
August 2012
Institut de Recherche Interdisciplinaire (IRIBHM), Université Libre de Bruxelles, Campus Erasme, Brussels, Belgium.
Phosphoinositide (PI) phosphatases such as the SH2 domain-containing inositol 5-phosphatases 1/2 (SHIP1 and 2) are important signalling enzymes in human physiopathology. SHIP1/2 interact with a large number of immune and growth factor receptors. Tyrosine phosphorylation of SHIP1/2 has been considered to be the determining regulatory modification.
View Article and Find Full Text PDFSHIP1/2 interaction with tyrosine phosphorylated peptides mimicking an immunoreceptor signalling motif.
Adv Enzyme Regul
January 2007
Interdisciplinary Research Institute (IRIBHM), Université Libre de Bruxelles, Campus Erasme, Bldg C, 808 Route de Lennik, 1070 Brussels, Belgium.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!