PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 18690034-0 2007 Exaggerated Mg2+ inhibition of Kir2.1 as a consequence of reduced PIP2 sensitivity in Andersen syndrome. Phosphatidylinositol 4,5-Diphosphate 66-70 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 31-37 18725531-4 2008 Homology modeling of this putative PIP(2)-binding linker in Kv7.2 and Kv7.3 using the solved structure of Kir2.1 and Kir3.1 channels as templates predicts a structure of Kv7.2 and 7.3 very similar to the Kir channels, and to the seven-beta-sheet barrel motif common to other PIP(2)-binding domains. Phosphatidylinositol 4,5-Diphosphate 35-41 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 106-112 18725531-4 2008 Homology modeling of this putative PIP(2)-binding linker in Kv7.2 and Kv7.3 using the solved structure of Kir2.1 and Kir3.1 channels as templates predicts a structure of Kv7.2 and 7.3 very similar to the Kir channels, and to the seven-beta-sheet barrel motif common to other PIP(2)-binding domains. Phosphatidylinositol 4,5-Diphosphate 275-281 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 106-112 18690051-6 2008 Moreover, by controlling the number of PIP(2)-sensitive subunits in the stoichiometry of a tetrameric Kir2.1 channel, we showed that characteristic channel activity was obtained when at least two wild-type subunits were present. Phosphatidylinositol 4,5-Diphosphate 39-45 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 102-108 16316973-0 2005 Long polyamines act as cofactors in PIP2 activation of inward rectifier potassium (Kir2.1) channels. Phosphatidylinositol 4,5-Diphosphate 36-40 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 83-89 16316973-4 2005 Here we show that polyamines, which cause inward rectification by selectively blocking outward current, also regulate the interaction of PIP2 with Kir2.1 channels to maintain channel availability. Phosphatidylinositol 4,5-Diphosphate 137-141 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 147-153 16316973-10 2005 We conclude that long polyamines serve a dual role as both blockers and coactivators (with PIP2) of Kir2.1 channels. Phosphatidylinositol 4,5-Diphosphate 91-95 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 100-106 16217063-9 2005 CONCLUSION: Six new disease-causing mutations in KCNJ2 were identified, one of which was in a PIP2 binding site. Phosphatidylinositol 4,5-Diphosphate 94-98 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 49-54 16260839-7 2005 These same positively charged ions inhibited IRK1 current in parallel with MIC current, suggesting that they probably act by screening the head group phosphates on PIP2 and other membrane phospholipids. Phosphatidylinositol 4,5-Diphosphate 164-168 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 45-49 12475570-2 2003 Kir2.1 (classical inward rectifier K(+) channel), Kir6.2/SUR2A (ATP-sensitive K(+) channel) and Kir3.1/3.4 (muscarinic K(+) channels) in cardiac myocytes are commonly upregulated by a membrane lipid, phosphatidylinositol 4,5-bisphosphates (PIP(2)). Phosphatidylinositol 4,5-Diphosphate 200-238 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 0-6 15980413-6 2005 Biochemical studies also demonstrate that PIP2 and LC-CoA bind with similar affinity to the C-terminal domains of Kir2.1 and Kir6.2 and that PIP2 binding can be competitively antagonized by LC-CoA, suggesting that the mechanism of LC-CoA inhibition involves displacement of PIP2. Phosphatidylinositol 4,5-Diphosphate 42-46 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 114-120 12796536-0 2003 PIP2 binding residues of Kir2.1 are common targets of mutations causing Andersen syndrome. Phosphatidylinositol 4,5-Diphosphate 0-4 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 25-31 12796536-10 2003 CONCLUSIONS: The novel mutations corresponding to residues involved in Kir2.1 channel-PIP2 interactions presented here as well as the overall frequency of mutations occurring in these residues indicate that defects in PIP2 binding constitute a major pathogenic mechanism of ATS. Phosphatidylinositol 4,5-Diphosphate 86-90 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 71-77 11353868-7 2001 Surprisingly, GIRK1/2 channels with high affinity for PIP(2) were inhibited by ethanol, like IRK1 channels. Phosphatidylinositol 4,5-Diphosphate 54-60 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 15-19 11353868-6 2001 The mutated GIRK1 and GIRK2 (GIRK1/2) channels containing the high-affinity phosphatidylinositol 4,5-bisphosphate (PIP(2)) domain from IRK1, on the other hand, showed dramatically less inhibition with bupivacaine. Phosphatidylinositol 4,5-Diphosphate 76-113 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 13-17 11172809-0 2001 Multiple PIP2 binding sites in Kir2.1 inwardly rectifying potassium channels. Phosphatidylinositol 4,5-Diphosphate 9-13 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 31-37 11172809-2 2001 Three independent sites (aa 175-206, aa 207-246, aa 324-365) were located in the C-terminal domain of Kir2.1 channels by assaying the binding of overlapping fragments to PIP2 containing liposomes. Phosphatidylinositol 4,5-Diphosphate 170-174 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 102-108 9486652-6 1998 Consistent with the faster dissociation of PIP2 from the GIRK channels, the carboxy terminus of GIRK1 binds 3H-PIP2 liposomes more weakly than does that of IRK1 or ROMK1. Phosphatidylinositol 4,5-Diphosphate 43-47 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 97-101 10559906-1 1999 Direct interactions of phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) with inwardly rectifying potassium channels are stronger with channels rendered constitutively active by binding to PtdIns(4,5)P2, such as IRK1, than with G-protein-gated channels (GIRKs). Phosphatidylinositol 4,5-Diphosphate 23-60 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 216-220 10559906-1 1999 Direct interactions of phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) with inwardly rectifying potassium channels are stronger with channels rendered constitutively active by binding to PtdIns(4,5)P2, such as IRK1, than with G-protein-gated channels (GIRKs). Phosphatidylinositol 4,5-Diphosphate 62-75 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 216-220 10559906-1 1999 Direct interactions of phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) with inwardly rectifying potassium channels are stronger with channels rendered constitutively active by binding to PtdIns(4,5)P2, such as IRK1, than with G-protein-gated channels (GIRKs). Phosphatidylinositol 4,5-Diphosphate 193-206 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 216-220 10559906-2 1999 As a result, PtdIns(4,5)P2 alone can activate IRK1 but not GIRKs, which require extra gating molecules such as the beta gamma subunits of G proteins or sodium ions. Phosphatidylinositol 4,5-Diphosphate 13-26 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 46-50 10559906-4 1999 Between these two arginines, a conservative change of isoleucine residue 229 in GIRK4 to the corresponding leucine found in IRK1 strengthens GIRK4-PtdIns(4,5)P2 interactions, eliminating the need for extra gating molecules. Phosphatidylinositol 4,5-Diphosphate 147-160 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 124-128 33151169-6 2021 Additionally, the PIP2 intracellular application had largely reduced the inhibition of Kir2.1 channels by terfenadine. Phosphatidylinositol 4,5-Diphosphate 18-22 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 87-93 28660286-7 2017 Molecular docking results determine that HA binds with Kir2.1 at K182, K185, and K188, which are phosphatidylinositol 4,5-bisphosphate (PIP2) binding residues. Phosphatidylinositol 4,5-Diphosphate 97-134 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 55-61 29581272-3 2018 Here, we identify a key regulator of this process, demonstrating that phosphatidylinositol 4,5-bisphosphate (PIP2) is an intrinsic modulator of capillary Kir2.1-mediated signaling. Phosphatidylinositol 4,5-Diphosphate 70-107 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 154-160 29581272-3 2018 Here, we identify a key regulator of this process, demonstrating that phosphatidylinositol 4,5-bisphosphate (PIP2) is an intrinsic modulator of capillary Kir2.1-mediated signaling. Phosphatidylinositol 4,5-Diphosphate 109-113 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 154-160 29581272-5 2018 These results collectively show that PIP2 sets the gain of capillary-initiated electrical signaling by modulating Kir2.1 channels. Phosphatidylinositol 4,5-Diphosphate 37-41 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 114-120 33050503-5 2020 It is found that Kir2.1 membrane expression and anchoring are associated with PIP2 affinity, and PIP2 depletion inhibits actin filament dynamics. Phosphatidylinositol 4,5-Diphosphate 78-82 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 17-23 28660286-7 2017 Molecular docking results determine that HA binds with Kir2.1 at K182, K185, and K188, which are phosphatidylinositol 4,5-bisphosphate (PIP2) binding residues. Phosphatidylinositol 4,5-Diphosphate 136-140 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 55-61 28660286-8 2017 Our results indicate that HA competes with PIP2 to bind with Kir2.1 and inhibits the currents. Phosphatidylinositol 4,5-Diphosphate 43-47 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 61-67 28446610-4 2017 In Kir2.1, mutation of one of these CD-I salt bridge residues (R204A) reduces apparent PIP2 sensitivity of channel activity, and here we show that Ala or Cys substitutions of the functionally equivalent residue (Arg-165) in the prokaryotic Kir channel KirBac1.1 also significantly decrease sensitivity of the channel to PIP2 (by 5-30-fold). Phosphatidylinositol 4,5-Diphosphate 87-91 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 3-9 28389584-8 2017 Kir2.1 channels contain homologous salt bridges, and we find that mutations that disrupt CD-I interactions in Kir2.1 also reduce channel activity and PIP2 sensitivity. Phosphatidylinositol 4,5-Diphosphate 150-154 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 0-6 28188270-12 2017 Inversely, mutant channels interacting only weakly with PIP2 (i.e., Kir2.1 K182Q, and L221I) are prone to a higher inhibitory effect. Phosphatidylinositol 4,5-Diphosphate 56-60 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 68-74 28389584-8 2017 Kir2.1 channels contain homologous salt bridges, and we find that mutations that disrupt CD-I interactions in Kir2.1 also reduce channel activity and PIP2 sensitivity. Phosphatidylinositol 4,5-Diphosphate 150-154 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 110-116 20921230-2 2010 We have characterized the PIP(2) dependence of purified human Kir2.1 and Kir2.2 activity using (86)Rb(+) flux and patch clamp assays in liposomes of defined composition. Phosphatidylinositol 4,5-Diphosphate 26-32 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 62-68 27527100-2 2016 Phosphatidylinositol-4,5-bisphosphate (PIP2) binding to a primary site is required for opening of classic inward rectifier Kir2.1 and Kir2.2 channels, but interaction of bulk anionic phospholipid (PL(-)) with a distinct second site is required for high PIP2 sensitivity. Phosphatidylinositol 4,5-Diphosphate 0-37 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 123-129 27527100-2 2016 Phosphatidylinositol-4,5-bisphosphate (PIP2) binding to a primary site is required for opening of classic inward rectifier Kir2.1 and Kir2.2 channels, but interaction of bulk anionic phospholipid (PL(-)) with a distinct second site is required for high PIP2 sensitivity. Phosphatidylinositol 4,5-Diphosphate 39-43 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 123-129 21281576-3 2011 Our results demonstrate that Kir2.1 and Kir2.2 have two distinct lipid requirements for activity: a specific requirement for phosphatidylinositol 4,5-bisphosphate (PIP(2)) and a nonspecific requirement for anionic phospholipids. Phosphatidylinositol 4,5-Diphosphate 125-162 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 29-35 20921230-4 2010 The results provide the first quantitative description of the dependence of eukaryotic Kir channel function on PIP(2) levels in the membrane; Kir2.1 shows measureable activity in as little as 0.01% PIP(2), and open probability increases to ~0.4 at 1% PIP(2). Phosphatidylinositol 4,5-Diphosphate 111-117 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 142-148 20921230-5 2010 Activation of Kir2.1 by phosphatidylinositol phosphates is also highly selective for PIP(2); PI, PI(4)P, and PI(5)P do not activate channels, and PI(3,4,5)P(3) causes minimal activity. Phosphatidylinositol 4,5-Diphosphate 85-91 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 14-20 19654266-12 2009 Pretreatment with spermine (100 microM) decreased the inhibitory effect of tamoxifen on Kir2.1, probably by strengthening the channel"s interaction with PIP(2). Phosphatidylinositol 4,5-Diphosphate 153-159 potassium inwardly rectifying channel subfamily J member 2 Homo sapiens 88-94