PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15037311-7 2004 Finally, PIP2 also stimulates the transient, direct binding interaction of the Arp2/3 complex with vinculin and thus may couple adhesion to actin assembly. Phosphatidylinositol 4,5-Diphosphate 9-13 vinculin Homo sapiens 99-107 22824265-4 2012 The simulations demonstrate that once each phosphorylated vinculin structure is at equilibrium, significant local conformational changes result that may impact either vinculin activation or vinculin binding to actin and PIP2. Phosphatidylinositol 4,5-Diphosphate 220-224 vinculin Homo sapiens 58-66 12422220-3 2002 Phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P(2)) regulates interactions between these proteins, including the interaction of vinculin with actin and talin. Phosphatidylinositol 4,5-Diphosphate 0-37 vinculin Homo sapiens 132-140 8632828-0 1996 Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate. Phosphatidylinositol 4,5-Diphosphate 53-91 vinculin Homo sapiens 14-22 34411575-0 2021 PIP2-induced membrane binding of the Vinculin tail competes with its other binding partners. Phosphatidylinositol 4,5-Diphosphate 0-4 vinculin Homo sapiens 37-45 34411575-1 2021 Vinculin plays a key role during the first phase of focal adhesion formation and interacts with the plasma membrane through specific binding of its Tail domain to the lipid phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 173-210 vinculin Homo sapiens 0-8 34411575-1 2021 Vinculin plays a key role during the first phase of focal adhesion formation and interacts with the plasma membrane through specific binding of its Tail domain to the lipid phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 212-216 vinculin Homo sapiens 0-8 34411575-4 2021 This allowed us to map the interaction of the Vinculin Tail with PIP2-enriched membranes at atomistic detail. Phosphatidylinositol 4,5-Diphosphate 65-69 vinculin Homo sapiens 46-54 34411575-9 2021 Importantly, many of these PIP2 binding residues are also involved in maintaining Vinculin in a closed, auto-inhibited conformation. Phosphatidylinositol 4,5-Diphosphate 27-31 vinculin Homo sapiens 82-90 29696730-4 2018 The aim of this short communication is to discuss whether the C-terminal vinculin tail (Vt) domain interacts favorably with membrane-embedded phospholipids such as PIP2 and that the region is also an anchor for lipid membranes. Phosphatidylinositol 4,5-Diphosphate 164-168 vinculin Homo sapiens 73-81 27705767-2 2016 Vinculin (Vn) is a major adaptor protein that regulates focal adhesions in conjunction with PIP2 in lipid membranes and other cytoskeletal components. Phosphatidylinositol 4,5-Diphosphate 92-96 vinculin Homo sapiens 0-8 27705767-2 2016 Vinculin (Vn) is a major adaptor protein that regulates focal adhesions in conjunction with PIP2 in lipid membranes and other cytoskeletal components. Phosphatidylinositol 4,5-Diphosphate 92-96 vinculin Homo sapiens 10-12 27705767-7 2016 Conversely, activated Vn binds strongly to membranes through specific interactions with clusters of PIP2 embedded in lipid membranes. Phosphatidylinositol 4,5-Diphosphate 100-104 vinculin Homo sapiens 22-24 27503891-5 2016 Contrary to studies that suggested that phosphoinositol-4,5-bisphosphate (PIP2) only induces vinculin homodimers, which are asymmetric, we show that phospholipid binding results in a domain-swapped symmetric MV dimer via a quasi-equivalent interface compared with vinculin involving R975. Phosphatidylinositol 4,5-Diphosphate 74-78 vinculin Homo sapiens 93-101 27503891-5 2016 Contrary to studies that suggested that phosphoinositol-4,5-bisphosphate (PIP2) only induces vinculin homodimers, which are asymmetric, we show that phospholipid binding results in a domain-swapped symmetric MV dimer via a quasi-equivalent interface compared with vinculin involving R975. Phosphatidylinositol 4,5-Diphosphate 74-78 vinculin Homo sapiens 264-272 25880222-3 2015 At the plasma cell membrane, the most abundant phosphoinositide, phosphatidylinositol 4,5-bisphosphate (PIP2), binds the vinculin tail domain, Vt, and triggers homotypic and heterotypic interactions that amplify binding of vinculin to the actin network. Phosphatidylinositol 4,5-Diphosphate 65-102 vinculin Homo sapiens 121-129 25880222-3 2015 At the plasma cell membrane, the most abundant phosphoinositide, phosphatidylinositol 4,5-bisphosphate (PIP2), binds the vinculin tail domain, Vt, and triggers homotypic and heterotypic interactions that amplify binding of vinculin to the actin network. Phosphatidylinositol 4,5-Diphosphate 65-102 vinculin Homo sapiens 223-231 25880222-3 2015 At the plasma cell membrane, the most abundant phosphoinositide, phosphatidylinositol 4,5-bisphosphate (PIP2), binds the vinculin tail domain, Vt, and triggers homotypic and heterotypic interactions that amplify binding of vinculin to the actin network. Phosphatidylinositol 4,5-Diphosphate 104-108 vinculin Homo sapiens 121-129 25880222-3 2015 At the plasma cell membrane, the most abundant phosphoinositide, phosphatidylinositol 4,5-bisphosphate (PIP2), binds the vinculin tail domain, Vt, and triggers homotypic and heterotypic interactions that amplify binding of vinculin to the actin network. Phosphatidylinositol 4,5-Diphosphate 104-108 vinculin Homo sapiens 223-231 25880222-4 2015 Binding of PIP2 to Vt is necessary for maintaining optimal focal adhesions, for organizing stress fibers, for cell migration and spreading, and for the control of vinculin dynamics and turnover of focal adhesions. Phosphatidylinositol 4,5-Diphosphate 11-15 vinculin Homo sapiens 163-171 25880222-6 2015 Here, via a series of novel biochemical assays not performed in previous studies that relied on chemical cross-linking, we characterize the PIP2-induced vinculin oligomerization. Phosphatidylinositol 4,5-Diphosphate 140-144 vinculin Homo sapiens 153-161 25241342-2 2014 It is accepted that when cells adhere to the extracellular matrix, a part of the soluble cytosolic pool of vinculin is recruited to specialized sites on the plasma membrane called focal adhesions (FAs) by binding to plasma membrane phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2). Phosphatidylinositol 4,5-Diphosphate 232-269 vinculin Homo sapiens 107-115 25241342-2 2014 It is accepted that when cells adhere to the extracellular matrix, a part of the soluble cytosolic pool of vinculin is recruited to specialized sites on the plasma membrane called focal adhesions (FAs) by binding to plasma membrane phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2). Phosphatidylinositol 4,5-Diphosphate 271-284 vinculin Homo sapiens 107-115 25241342-3 2014 We have previously shown that bradykinin (BK) induces both a reversible dissipation of vinculin from FAs, by the phospholipase C (PLC)-mediated hydrolysis of PtdIns(4,5)P2, and the concomitant internalization of vinculin. Phosphatidylinositol 4,5-Diphosphate 158-171 vinculin Homo sapiens 87-95 9560340-0 1998 The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate. Phosphatidylinositol 4,5-Diphosphate 79-116 vinculin Homo sapiens 54-62 9560340-6 1998 Consistent with the view that vinculin must be activated at these sites, we found that PIP2, levels of which are elevated during the early stages of adhesion, bound to two discrete regions in the vinculin tail, disrupting the intramolecular head-tail interaction and inducing vinculin oligomerization. Phosphatidylinositol 4,5-Diphosphate 87-91 vinculin Homo sapiens 30-38 9560340-6 1998 Consistent with the view that vinculin must be activated at these sites, we found that PIP2, levels of which are elevated during the early stages of adhesion, bound to two discrete regions in the vinculin tail, disrupting the intramolecular head-tail interaction and inducing vinculin oligomerization. Phosphatidylinositol 4,5-Diphosphate 87-91 vinculin Homo sapiens 196-204 9560340-6 1998 Consistent with the view that vinculin must be activated at these sites, we found that PIP2, levels of which are elevated during the early stages of adhesion, bound to two discrete regions in the vinculin tail, disrupting the intramolecular head-tail interaction and inducing vinculin oligomerization. Phosphatidylinositol 4,5-Diphosphate 87-91 vinculin Homo sapiens 196-204 9560340-7 1998 Vinculin-VASP complex formation was greatly enhanced by PIP2 and both the EVH1 and EVH2 domains of VASP participated in vinculin binding. Phosphatidylinositol 4,5-Diphosphate 56-60 vinculin Homo sapiens 0-8 9560340-7 1998 Vinculin-VASP complex formation was greatly enhanced by PIP2 and both the EVH1 and EVH2 domains of VASP participated in vinculin binding. Phosphatidylinositol 4,5-Diphosphate 56-60 vinculin Homo sapiens 120-128 9560340-8 1998 CONCLUSIONS: Focal contact assembly involves interaction between VASP and vinculin, which is enhanced by PIP2-induced vinculin activation and oligomerization. Phosphatidylinositol 4,5-Diphosphate 105-109 vinculin Homo sapiens 74-82 9560340-8 1998 CONCLUSIONS: Focal contact assembly involves interaction between VASP and vinculin, which is enhanced by PIP2-induced vinculin activation and oligomerization. Phosphatidylinositol 4,5-Diphosphate 105-109 vinculin Homo sapiens 118-126 9560340-10 1998 We propose that PIP2-dependent signalling modulates microfilament organization at cellular adhesion sites by regulating vinculin-VASP complexes. Phosphatidylinositol 4,5-Diphosphate 16-20 vinculin Homo sapiens 120-128 21931851-8 2011 Taken together, PIPKIgamma positively regulates focal adhesion dynamics and cancer invasion, most probably through PIP2-mediated vinculin activation. Phosphatidylinositol 4,5-Diphosphate 115-119 vinculin Homo sapiens 129-137 19759271-5 2009 Regarding the reassembly of vinculin-stained FAs, we found that BK induces the formation of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2]-enriched vinculin-containing vesicles, which, by following a polarized exocytic route, transport vinculin to the site of FA assembly, an action that depends on actin filaments. Phosphatidylinositol 4,5-Diphosphate 92-129 vinculin Homo sapiens 28-36 19759271-5 2009 Regarding the reassembly of vinculin-stained FAs, we found that BK induces the formation of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2]-enriched vinculin-containing vesicles, which, by following a polarized exocytic route, transport vinculin to the site of FA assembly, an action that depends on actin filaments. Phosphatidylinositol 4,5-Diphosphate 92-129 vinculin Homo sapiens 155-163 19759271-5 2009 Regarding the reassembly of vinculin-stained FAs, we found that BK induces the formation of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2]-enriched vinculin-containing vesicles, which, by following a polarized exocytic route, transport vinculin to the site of FA assembly, an action that depends on actin filaments. Phosphatidylinositol 4,5-Diphosphate 92-129 vinculin Homo sapiens 155-163 19759271-5 2009 Regarding the reassembly of vinculin-stained FAs, we found that BK induces the formation of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2]-enriched vinculin-containing vesicles, which, by following a polarized exocytic route, transport vinculin to the site of FA assembly, an action that depends on actin filaments. Phosphatidylinositol 4,5-Diphosphate 131-144 vinculin Homo sapiens 28-36 19759271-5 2009 Regarding the reassembly of vinculin-stained FAs, we found that BK induces the formation of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2]-enriched vinculin-containing vesicles, which, by following a polarized exocytic route, transport vinculin to the site of FA assembly, an action that depends on actin filaments. Phosphatidylinositol 4,5-Diphosphate 131-144 vinculin Homo sapiens 155-163 19759271-5 2009 Regarding the reassembly of vinculin-stained FAs, we found that BK induces the formation of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2]-enriched vinculin-containing vesicles, which, by following a polarized exocytic route, transport vinculin to the site of FA assembly, an action that depends on actin filaments. Phosphatidylinositol 4,5-Diphosphate 131-144 vinculin Homo sapiens 155-163 19759271-6 2009 The present study, which was carried out with cells that were not genetically manipulated, shows for the first time that BK induces the formation of vesicle-like structures containing vinculin and PtdIns(4,5)P2, which transport vinculin to the site of FA assembly. Phosphatidylinositol 4,5-Diphosphate 197-210 vinculin Homo sapiens 228-236