PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11993989-2 2002 In the yeast SNARE protein Vam7p, the PX domain binds to PtdIns(3)P and is required for vacuolar targeting. phosphatidylinositol 3-phosphate 57-67 Vam7p Saccharomyces cerevisiae S288C 27-32 23071309-3 2012 The N-domain of the yeast vacuolar Qc-SNARE Vam7p is a binding partner for the homotypic fusion and vacuole protein sorting complex (a master regulator of vacuole fusion) and has Phox homology, providing a phosphatidylinositol 3-phosphate (PI3P)-specific membrane anchor. phosphatidylinositol 3-phosphate 206-238 Vam7p Saccharomyces cerevisiae S288C 44-49 20937838-4 2010 Using assays of membrane tethering, trans-SNARE pairing, and lipid mixing, we found that PI(3)P and PI(4,5)P(2) have distinct functions that are asymmetric with respect to R-SNARE (Nyv1p) and the 3Q-SNAREs (Vam3p, Vti1p, and Vam7p). phosphatidylinositol 3-phosphate 89-95 Vam7p Saccharomyces cerevisiae S288C 225-230 20937838-6 2010 PI(3)P on Q-SNARE proteoliposomes promoted Vam7p binding and association with the other two Q-SNAREs. phosphatidylinositol 3-phosphate 0-6 Vam7p Saccharomyces cerevisiae S288C 43-48 20937838-7 2010 PI(3)P on R-SNARE proteoliposomes was recognized by the PX domain of Vam7p on Q-SNARE proteoliposomes to promote tethering, although this function could be supplanted by the tethering activity of HOPS. phosphatidylinositol 3-phosphate 0-6 Vam7p Saccharomyces cerevisiae S288C 69-74 16877709-3 2006 For example, Vam7p is targeted by its PX domain to phosphatidylinositol 3-phosphate [PtdIns(3)P] in the yeast vacuole, where it interacts with other SNARE proteins and GTPases of the vesicular membrane fusion machinery. phosphatidylinositol 3-phosphate 51-83 Vam7p Saccharomyces cerevisiae S288C 13-18 16877709-3 2006 For example, Vam7p is targeted by its PX domain to phosphatidylinositol 3-phosphate [PtdIns(3)P] in the yeast vacuole, where it interacts with other SNARE proteins and GTPases of the vesicular membrane fusion machinery. phosphatidylinositol 3-phosphate 85-95 Vam7p Saccharomyces cerevisiae S288C 13-18 23955338-4 2013 Using pure components that are active in reconstituted vacuolar fusion, we now find that Vam7p binds to membranes through its combined affinities for several vacuolar membrane constituents: HOPS, phosphatidylinositol 3-phosphate, SNAREs, and acidic phospholipids. phosphatidylinositol 3-phosphate 196-228 Vam7p Saccharomyces cerevisiae S288C 89-94 17347148-3 2007 One SNARE, Vam7p, has an N-terminal PX domain which binds to phosphatidylinositol 3-phosphate (PI(3)P) and to HOPS and a C-terminal SNARE domain but no apolar membrane anchor. phosphatidylinositol 3-phosphate 61-93 Vam7p Saccharomyces cerevisiae S288C 11-16 17347148-3 2007 One SNARE, Vam7p, has an N-terminal PX domain which binds to phosphatidylinositol 3-phosphate (PI(3)P) and to HOPS and a C-terminal SNARE domain but no apolar membrane anchor. phosphatidylinositol 3-phosphate 95-101 Vam7p Saccharomyces cerevisiae S288C 11-16 17347148-5 2007 Lowering the PI(3)P affinity of the PX domain, or even deleting the PX domain, affects the fusion K(m) for Vam7p but not the maximal fusion rate. phosphatidylinositol 3-phosphate 13-19 Vam7p Saccharomyces cerevisiae S288C 107-112 11993989-4 2002 The Vam7p PX domain has the same overall alpha/beta fold observed in the structures of the ligand-free p47(phox) PX domain and the PtdIns(3)P-bound p40(phox) PX domain, exhibiting several similarities and differences with these two PX domains. phosphatidylinositol 3-phosphate 131-141 Vam7p Saccharomyces cerevisiae S288C 4-9 11993989-6 2002 These similarities and the observation that a putative PtdIns(3)P binding site is already formed in the apo Vam7p PX domains suggest that ligand binding does not induce major conformational changes, contrary to what was previously thought. phosphatidylinositol 3-phosphate 55-65 Vam7p Saccharomyces cerevisiae S288C 108-113 11993989-7 2002 The proposed ligand binding site of the Vam7p PX domain includes basic side chains from the conserved structural core that also participate in PtdIns(3)P binding to the p40(phox) PX domain, and basic side chains from a variable loop that probably inserts into the membrane. phosphatidylinositol 3-phosphate 143-153 Vam7p Saccharomyces cerevisiae S288C 40-45 11916982-5 2002 Both the recombinant Vam7p PX domain and a FYVE domain construct of human Hrs block the recruitment of Vam7p and vacuole fusion, demonstrating that phosphatidylinositol 3-phosphate is a primary receptor of Vam7p on vacuoles. phosphatidylinositol 3-phosphate 148-180 Vam7p Saccharomyces cerevisiae S288C 21-26 11916982-5 2002 Both the recombinant Vam7p PX domain and a FYVE domain construct of human Hrs block the recruitment of Vam7p and vacuole fusion, demonstrating that phosphatidylinositol 3-phosphate is a primary receptor of Vam7p on vacuoles. phosphatidylinositol 3-phosphate 148-180 Vam7p Saccharomyces cerevisiae S288C 103-108 11916982-5 2002 Both the recombinant Vam7p PX domain and a FYVE domain construct of human Hrs block the recruitment of Vam7p and vacuole fusion, demonstrating that phosphatidylinositol 3-phosphate is a primary receptor of Vam7p on vacuoles. phosphatidylinositol 3-phosphate 148-180 Vam7p Saccharomyces cerevisiae S288C 103-108 11433291-0 2001 Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes. phosphatidylinositol 3-phosphate 29-39 Vam7p Saccharomyces cerevisiae S288C 52-56 11433291-3 2001 Here, we show that the PX domain of Vam7 targets to vacuoles in vivo in a manner dependent on phosphatidylinositol 3-phosphate generation. phosphatidylinositol 3-phosphate 94-126 Vam7p Saccharomyces cerevisiae S288C 36-40 27365394-0 2016 The Central Polybasic Region of the Soluble SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Vam7 Affects Binding to Phosphatidylinositol 3-Phosphate by the PX (Phox Homology) Domain. phosphatidylinositol 3-phosphate 146-178 Vam7p Saccharomyces cerevisiae S288C 122-126 27365394-2 2016 The N-terminal PX domain of Vam7 binds to the lipid phosphatidylinositol 3-phosphate (PI3P) and the tethering complex HOPS (homotypic fusion and vacuole protein sorting complex), whereas the C-terminal SNARE motif forms SNARE complexes. phosphatidylinositol 3-phosphate 52-84 Vam7p Saccharomyces cerevisiae S288C 28-32