DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, SK | - |
dc.contributor.author | Wee, SM | - |
dc.contributor.author | Chang, JS | - |
dc.contributor.author | Kwon, TK | - |
dc.contributor.author | Min, DS | - |
dc.contributor.author | Lee, YH | - |
dc.contributor.author | Suh, PG | - |
dc.date.accessioned | 2016-04-01T02:19:07Z | - |
dc.date.available | 2016-04-01T02:19:07Z | - |
dc.date.created | 2009-02-28 | - |
dc.date.issued | 2004-11-30 | - |
dc.identifier.issn | 1225-8687 | - |
dc.identifier.other | 2005-OAK-0000004708 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/24902 | - |
dc.description.abstract | A nuzmber of signaling molecules contain small pleckstrin homology (PH) domains capable of binding phosphoinositides; or proteins. Phospholipase C (PLC)-gamma1 has two putative PH domains, an NH2-terminal (PH1) and a split PH domain (nPH(2) and cPH(2)). We previously reported that the split PH domain of PLC-gamma1 binds to phosphatidylinositol 4-phosphate (PI(4)P) and phosphatidylinositol 4,5-bisphosphate (PI(4,5)P,) (Chang et A, 2002). To identify the amino acid residues responsible for binding with PI(4)P and PI(4,5)P-2, we used site-directed mutagenesis to replace each amino acid in the variable loop-1 (VL-1) region of the PLC-gamma1 nPH(2) domain with alanine (a neutral amino acid). The phosphoinositide-binding affinity of these mutant molecules was analyzed by Dot-blot assay followed by ECL detection. We found that two PLC-gamma1 nPH(2) domain mutants, P500A and H503A, showed reduced affinities for phosphoinositide binding. Furthermore, these mutant PLC-gamma1 molecules showed reduced PI(4,5)P, hydrolysis. Using green fluorescent protein (GFP) fusion protein system, we showed that both PH1 and nPH(2) domains are responsible for membrane-targeted translocation of PLC-gamma1 upon serum stimulation. Together, our data reveal that the amino acid residues Pro(500) and His(503) are critical for binding of PLC-gamma1 to one of its substrates, PI(4,5)P, in the membrane. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | SPRINGER SINGAPORE PTE LTD | - |
dc.relation.isPartOf | JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY | - |
dc.subject | dot-blottin | - |
dc.subject | phosphatidylinositol 4,5-bisphosphate | - |
dc.subject | phospholipase C-gamma l | - |
dc.subject | pleckstrin homology domain | - |
dc.subject | proteinphosphoinositide interaction | - |
dc.subject | PLECKSTRIN HOMOLOGY DOMAINS | - |
dc.subject | PHOSPHOLIPASE C-GAMMA | - |
dc.subject | PROTEIN-KINASE-C | - |
dc.subject | COMMON FOLD | - |
dc.subject | OVEREXPRESSION | - |
dc.subject | ASSOCIATION | - |
dc.subject | ACTIVATION | - |
dc.subject | C-GAMMA-1 | - |
dc.subject | SEQUENCES | - |
dc.subject | SUBUNITS | - |
dc.title | Point mutations in the split PLC-gamma 1 PH domain modulate phosphoinositide binding | - |
dc.type | Article | - |
dc.contributor.college | 생명과학과 | - |
dc.author.google | Kim, SK | - |
dc.author.google | Wee, SM | - |
dc.author.google | Chang, JS | - |
dc.author.google | Kwon, TK | - |
dc.author.google | Min, DS | - |
dc.author.google | Lee, YH | - |
dc.author.google | Suh, PG | - |
dc.relation.volume | 37 | - |
dc.relation.issue | 6 | - |
dc.relation.startpage | 720 | - |
dc.relation.lastpage | 725 | - |
dc.contributor.id | 10052640 | - |
dc.relation.journal | JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCIE | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.37, no.6, pp.720 - 725 | - |
dc.identifier.wosid | 000225443200013 | - |
dc.date.tcdate | 2019-02-01 | - |
dc.citation.endPage | 725 | - |
dc.citation.number | 6 | - |
dc.citation.startPage | 720 | - |
dc.citation.title | JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY | - |
dc.citation.volume | 37 | - |
dc.contributor.affiliatedAuthor | Suh, PG | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 5 | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | PLECKSTRIN HOMOLOGY DOMAINS | - |
dc.subject.keywordPlus | PHOSPHOLIPASE C-GAMMA | - |
dc.subject.keywordPlus | PROTEIN-KINASE-C | - |
dc.subject.keywordPlus | COMMON FOLD | - |
dc.subject.keywordPlus | OVEREXPRESSION | - |
dc.subject.keywordPlus | ASSOCIATION | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | C-GAMMA-1 | - |
dc.subject.keywordPlus | SEQUENCES | - |
dc.subject.keywordPlus | SUBUNITS | - |
dc.subject.keywordAuthor | dot-blottin | - |
dc.subject.keywordAuthor | phosphatidylinositol 4,5-bisphosphate | - |
dc.subject.keywordAuthor | phospholipase C-gamma l | - |
dc.subject.keywordAuthor | pleckstrin homology domain | - |
dc.subject.keywordAuthor | proteinphosphoinositide interaction | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
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