3nsu

From Proteopedia

(Difference between revisions)

Current revision

A Systematic Screen for Protein-Lipid Interactions in Saccharomyces cerevisiae

Structural highlights

3nsu is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SLM1_YEAST Together with SLM2, effector of the TORC2- and calcineurin-signaling pathways. Phosphorylated and activated by TORC2 under favorable growth conditions. Mediates actin polarization via inhibition of calcineurin-dependent transcription. Upon nutrient limitation or environmental stress, gets dephosphorylated by calcineurin. Dephosphorylation inhibits its interaction with TORC2, thereby antagonizing TORC2 signaling and mediating calcineurin-dependent actin depolarization. Also functions in heat-induced, calcineurin-mediated uracil permease (FUR4) endocytosis.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Protein-metabolite networks are central to biological systems, but are incompletely understood. Here, we report a screen to catalog protein-lipid interactions in yeast. We used arrays of 56 metabolites to measure lipid-binding fingerprints of 172 proteins, including 91 with predicted lipid-binding domains. We identified 530 protein-lipid associations, the majority of which are novel. To show the data set's biological value, we studied further several novel interactions with sphingolipids, a class of conserved bioactive lipids with an elusive mode of action. Integration of live-cell imaging suggests new cellular targets for these molecules, including several with pleckstrin homology (PH) domains. Validated interactions with Slm1, a regulator of actin polarization, show that PH domains can have unexpected lipid-binding specificities and can act as coincidence sensors for both phosphatidylinositol phosphates and phosphorylated sphingolipids.

A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae.,Gallego O, Betts MJ, Gvozdenovic-Jeremic J, Maeda K, Matetzki C, Aguilar-Gurrieri C, Beltran-Alvarez P, Bonn S, Fernandez-Tornero C, Jensen LJ, Kuhn M, Trott J, Rybin V, Muller CW, Bork P, Kaksonen M, Russell RB, Gavin AC Mol Syst Biol. 2010 Nov 30;6:430. PMID:21119626^[5]

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

References

↑ Audhya A, Loewith R, Parsons AB, Gao L, Tabuchi M, Zhou H, Boone C, Hall MN, Emr SD. Genome-wide lethality screen identifies new PI4,5P2 effectors that regulate the actin cytoskeleton. EMBO J. 2004 Oct 1;23(19):3747-57. Epub 2004 Sep 16. PMID:15372071 doi:10.1038/sj.emboj.7600384
↑ Fadri M, Daquinag A, Wang S, Xue T, Kunz J. The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2. Mol Biol Cell. 2005 Apr;16(4):1883-900. Epub 2005 Feb 2. PMID:15689497 doi:E04-07-0564
↑ Mulet JM, Martin DE, Loewith R, Hall MN. Mutual antagonism of target of rapamycin and calcineurin signaling. J Biol Chem. 2006 Nov 3;281(44):33000-7. Epub 2006 Sep 7. PMID:16959779 doi:M604244200
↑ Bultynck G, Heath VL, Majeed AP, Galan JM, Haguenauer-Tsapis R, Cyert MS. Slm1 and slm2 are novel substrates of the calcineurin phosphatase required for heat stress-induced endocytosis of the yeast uracil permease. Mol Cell Biol. 2006 Jun;26(12):4729-45. PMID:16738335 doi:10.1128/MCB.01973-05
↑ Gallego O, Betts MJ, Gvozdenovic-Jeremic J, Maeda K, Matetzki C, Aguilar-Gurrieri C, Beltran-Alvarez P, Bonn S, Fernandez-Tornero C, Jensen LJ, Kuhn M, Trott J, Rybin V, Muller CW, Bork P, Kaksonen M, Russell RB, Gavin AC. A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae. Mol Syst Biol. 2010 Nov 30;6:430. PMID:21119626 doi:10.1038/msb.2010.87

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3nsu"

@@ Line 1: / Line 1: @@
 ==A Systematic Screen for Protein-Lipid Interactions in Saccharomyces cerevisiae==
-<StructureSection load='3nsu' size='340' side='right' caption='[[3nsu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='3nsu' size='340' side='right'caption='[[3nsu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3nsu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NSU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NSU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3nsu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NSU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1btk|1btk]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LIT2, SLM1, YIL105C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=3nsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nsu OCA], [https://pdbe.org/3nsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nsu RCSB], [https://www.ebi.ac.uk/pdbsum/3nsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nsu ProSAT]</span></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=3nsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nsu OCA], [http://pdbe.org/3nsu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nsu RCSB], [http://www.ebi.ac.uk/pdbsum/3nsu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nsu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SLM1_YEAST SLM1_YEAST]] Together with SLM2, effector of the TORC2- and calcineurin-signaling pathways. Phosphorylated and activated by TORC2 under favorable growth conditions. Mediates actin polarization via inhibition of calcineurin-dependent transcription. Upon nutrient limitation or environmental stress, gets dephosphorylated by calcineurin. Dephosphorylation inhibits its interaction with TORC2, thereby antagonizing TORC2 signaling and mediating calcineurin-dependent actin depolarization. Also functions in heat-induced, calcineurin-mediated uracil permease (FUR4) endocytosis.<ref>PMID:15372071</ref> <ref>PMID:15689497</ref> <ref>PMID:16959779</ref> <ref>PMID:16738335</ref>
+[https://www.uniprot.org/uniprot/SLM1_YEAST SLM1_YEAST] Together with SLM2, effector of the TORC2- and calcineurin-signaling pathways. Phosphorylated and activated by TORC2 under favorable growth conditions. Mediates actin polarization via inhibition of calcineurin-dependent transcription. Upon nutrient limitation or environmental stress, gets dephosphorylated by calcineurin. Dephosphorylation inhibits its interaction with TORC2, thereby antagonizing TORC2 signaling and mediating calcineurin-dependent actin depolarization. Also functions in heat-induced, calcineurin-mediated uracil permease (FUR4) endocytosis.<ref>PMID:15372071</ref> <ref>PMID:15689497</ref> <ref>PMID:16959779</ref> <ref>PMID:16738335</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
+[[Category: Large Structures]]
-[[Category: Aguilar-Gurrieri, C]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Fernandez-Tornero, C]]
+[[Category: Aguilar-Gurrieri C]]
-[[Category: Gallego, O]]
+[[Category: Fernandez-Tornero C]]
-[[Category: Gavin, A C]]
+[[Category: Gallego O]]
-[[Category: Muller, C]]
+[[Category: Gavin AC]]
-[[Category: Pleckstrin homology domain]]
+[[Category: Muller C]]
-[[Category: Signaling protein]]

3nsu

From Proteopedia

Current revision

A Systematic Screen for Protein-Lipid Interactions in Saccharomyces cerevisiae

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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