The invention relates to proteins that bind to phosphatidylinositol 5-phosphate (PI(5)P). The invention also relates to the use of these proteins to measure and visualize PI(5)P in vivo and in vitro and as tools to investigate the role of PI(5)P in vivo.AURELIO TELEMAN...
Restricted Rac1 activation results from the binding of Tiam1 DH-PH domains to PtdIns5P. Using an assay that mimics Rac1 membrane anchoring by using Rac1-His and liposomes containing Ni2+-NTA modified lipids, we demonstrate that intrinsic Tiam1 DH-PH activity increases when Rac1 is anchored ...
The amino-terminal region of myotubularins contains a divergent PH domain [9] that might be a binding site for PtdIns5P, since arginine 69 of MTM1 lies within this domain and a basic residue is conserved at this position in other myotubularins. Consistent with this idea, another mutation at...
Phosphatidylinositol 5-phosphate 4-kinase (PI5P4K) is an enzyme activity capable of converting a monophosphorylated lipid substrate into a bisphosphorylated product, a reaction that is fundamental in the maintenance of the cellular phosphoinositide (PI) cycle. PI5P4K catalyzes the addition of a phosp...
(a) Septin 9 domain organization: the polybasic domain is located at N-terminal of GTP-binding domain, which is recognized by three motifs G1 (GXXXXGK ¼ G305QSGLGK311), G3 (DXXG ¼ D362TPG365), G4 (XKXD ¼ A444KAD447). Down: septin 9_i1 and septin 9_del1 sequence in...
Crystal structure of the phosphatidylinositol 3,4-bisphosphate-binding pleckstrin homology (PH) domain of tandem PH-domain-containing protein 1 (TAPP1): mo... Crystal structure of the phosphatidylinositol 3,4bisphosphate-binding pleckstrin homology (PH) domain of tandem PH-domain-containing protein 1...
At young seedling stages, the PIP5K3 and PIP5K4 genes responded to Pi deficiency in steady-state transcript levels via PHR1-binding sequences (P1BSs) in their upstream regions. Both pip5k3 and pip5k4 single mutants, which exhibit short-root-hair phenotypes, remained responsive to Pi ...
6C). This suggests that binding with NEDD4-1 is required for PIPKIγi5 to modulate Mig6 expression. PIPKIγi5KD still interacts with NEDD4-1 (Fig. 6B). This demonstrates that the kinase activity producing PtdIns(4,5)P2 is not required for PIPKIγi5-NEDD4-1 interaction. A series of ...
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This phosphorylation occurs in response to Fibronectin-RhoA signaling and leads to a decrease in PIP5Klγs' lipid kinase activity and binding affinity for Talin. Our data reveal a novel function for PKD1 as a regulator of FA dynamics and by identifying PIP5Klγ as a novel PKD1 substrate ...