| http://purl.uniprot.org/citations/16914545 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16914545 | http://www.w3.org/2000/01/rdf-schema#comment | "Myotubularins (MTM) are a large subfamily of lipid phosphatases that specifically dephosphorylate at the D3 position of phosphatidylinositol 3-phosphate (PI(3)P) in PI(3)P and PI(3,5)P2. We recently found that MTMR6 specifically inhibits the Ca2+-activated K+ channel, KCa3.1, by dephosphorylating PI(3)P. We now show that inhibition is specific for MTMR6 and other MTMs do not inhibit KCa3.1. By replacing either or both of the coiled-coil (CC) and pleckstrin homology/GRAM (PH/G) domains of MTMs that failed to inhibit KCa3.1 with the CC and PH/G domains of MTMR6, we found that chimeric MTMs containing both the MTMR6 CC and PH/G domains functioned like MTMR6 to inhibit KCa3.1 channel activity, whereas chimeric MTMs containing either domain alone did not. Immunofluorescent microscopy demonstrated that both the MTMR6 CC and PH/G domains are required to co-localize MTMR6 to the plasma membrane with KCa3.1. These findings support a model in which two specific low affinity interactions are required to co-localize MTMR6 with KCa3.1: 1) between the CC domains on MTMR6 and KCa3.1 and (2) between the PH/G domain and a component of the plasma membrane. Our inability to detect significant interaction of the MTMR6 G/PH domain with phosphoinositides suggests that this domain may bind a protein. Identifying the specific binding partners of the CC and PH/G domains on other MTMs will provide important clues to the specific functions regulated by other MTMs as well as the mechanism(s) whereby loss of some MTMs lead to disease."xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m606344200"xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/author | "Li Z."xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/author | "Srivastava S."xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/author | "Lemmon M.A."xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/author | "Choudhury P."xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/author | "Ko K."xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/author | "Narayan K."xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/author | "Skolnik E.Y."xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/author | "Coetzee W.A."xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/author | "Albaqumi M."xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/pages | "31762-31769"xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/title | "Specificity of the myotubularin family of phosphatidylinositol-3-phosphatase is determined by the PH/GRAM domain."xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://purl.uniprot.org/core/volume | "281"xsd:string |
| http://purl.uniprot.org/citations/16914545 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16914545 |
| http://purl.uniprot.org/citations/16914545 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16914545 |
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| http://purl.uniprot.org/uniprot/#_Q8NCE2-mappedCitation-16914545 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16914545 |