2kig: Difference between revisions

Latest revision as of 12:51, 20 December 2023

A PH domain within OCRL bridges clathrin mediated membrane trafficking to phosphoinositide metabolism

Structural highlights

2kig is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

I5P2_MOUSE Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events.^[1] ^[2]

Publication Abstract from PubMed

OCRL, whose mutations are responsible for Lowe syndrome and Dent disease, and INPP5B are two similar proteins comprising a central inositol 5-phosphatase domain followed by an ASH and a RhoGAP-like domain. Their divergent NH2-terminal portions remain uncharacterized. We show that the NH2-terminal region of OCRL, but not of INPP5B, binds clathrin heavy chain. OCRL, which in contrast to INPP5B visits late stage endocytic clathrin-coated pits, was earlier shown to contain another binding site for clathrin in its COOH-terminal region. NMR structure determination further reveals that despite their primary sequence dissimilarity, the NH2-terminal portions of both OCRL and INPP5B contain a PH domain. The novel clathrin-binding site in OCRL maps to an unusual clathrin-box motif located in a loop of the PH domain, whose mutations reduce recruitment efficiency of OCRL to coated pits. These findings suggest an evolutionary pressure for a specialized function of OCRL in bridging phosphoinositide metabolism to clathrin-dependent membrane trafficking.

A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism.,Mao Y, Balkin DM, Zoncu R, Erdmann KS, Tomasini L, Hu F, Jin MM, Hodsdon ME, De Camilli P EMBO J. 2009 Jul 8;28(13):1831-42. Epub 2009 Jun 18. PMID:19536138^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ O'Malley CJ, McColl BK, Kong AM, Ellis SL, Wijayaratnam AP, Sambrook J, Mitchell CA. Mammalian inositol polyphosphate 5-phosphatase II can compensate for the absence of all three yeast Sac1-like-domain-containing 5-phosphatases. Biochem J. 2001 May 1;355(Pt 3):805-17. PMID:11311145
↑ Matzaris M, O'Malley CJ, Badger A, Speed CJ, Bird PI, Mitchell CA. Distinct membrane and cytosolic forms of inositol polyphosphate 5-phosphatase II. Efficient membrane localization requires two discrete domains. J Biol Chem. 1998 Apr 3;273(14):8256-67. PMID:9525932
↑ Mao Y, Balkin DM, Zoncu R, Erdmann KS, Tomasini L, Hu F, Jin MM, Hodsdon ME, De Camilli P. A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism. EMBO J. 2009 Jul 8;28(13):1831-42. Epub 2009 Jun 18. PMID:19536138 doi:10.1038/emboj.2009.155

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] O'Malley CJ, McColl BK, Kong AM, Ellis SL, Wijayaratnam AP, Sambrook J, Mitchell CA. Mammalian inositol polyphosphate 5-phosphatase II can compensate for the absence of all three yeast Sac1-like-domain-containing 5-phosphatases. Biochem J. 2001 May 1;355(Pt 3):805-17. PMID:11311145

[2] Matzaris M, O'Malley CJ, Badger A, Speed CJ, Bird PI, Mitchell CA. Distinct membrane and cytosolic forms of inositol polyphosphate 5-phosphatase II. Efficient membrane localization requires two discrete domains. J Biol Chem. 1998 Apr 3;273(14):8256-67. PMID:9525932

[3] Mao Y, Balkin DM, Zoncu R, Erdmann KS, Tomasini L, Hu F, Jin MM, Hodsdon ME, De Camilli P. A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism. EMBO J. 2009 Jul 8;28(13):1831-42. Epub 2009 Jun 18. PMID:19536138 doi:10.1038/emboj.2009.155

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
 ==A PH domain within OCRL bridges clathrin mediated membrane trafficking to phosphoinositide metabolism==
-<StructureSection load='2kig' size='340' side='right' caption='[[2kig]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2kig' size='340' side='right'caption='[[2kig]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2kig]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KIG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KIG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2kig]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KIG FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Inpp5b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kig OCA], [http://pdbe.org/2kig PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kig RCSB], [http://www.ebi.ac.uk/pdbsum/2kig PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kig ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kig OCA], [https://pdbe.org/2kig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kig RCSB], [https://www.ebi.ac.uk/pdbsum/2kig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kig ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/I5P2_MOUSE I5P2_MOUSE]] Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events.<ref>PMID:11311145</ref> <ref>PMID:9525932</ref>
+[https://www.uniprot.org/uniprot/I5P2_MOUSE I5P2_MOUSE] Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events.<ref>PMID:11311145</ref> <ref>PMID:9525932</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 ==See Also==
 *[[Phosphoinositide phosphatase|Phosphoinositide phosphatase]]
+*[[3D structures of inositol polyphosphate 5-phosphatase OCRL|3D structures of inositol polyphosphate 5-phosphatase OCRL]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Camilli, P De]]
+[[Category: Mus musculus]]
-[[Category: Hodsdon, M E]]
+[[Category: De Camilli P]]
-[[Category: Mao, Y]]
+[[Category: Hodsdon ME]]
-[[Category: Clathrin]]
+[[Category: Mao Y]]
-[[Category: Endocytosis]]
-[[Category: Hydrolase]]
-[[Category: Inpp5b]]
-[[Category: Ocrl]]
-[[Category: Ph]]

2kig: Difference between revisions

Latest revision as of 12:51, 20 December 2023

A PH domain within OCRL bridges clathrin mediated membrane trafficking to phosphoinositide metabolism

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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