3g9g

From Proteopedia

(Difference between revisions)

Revision as of 17:07, 25 December 2014

Crystal Structure of the N-terminal EFC/F-BAR domain of Syp1

Structural highlights

3g9g is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3g9h
Gene:	SYP1, YCR030C, YCR30C/YCR29C (Saccharomyces cerevisiae)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[SYP1_YEAST] Multi-functional protein that contributes to the endocytic process, but also to events that occur at the neck during budding and/or cytokinesis. Plays a role as an endocytic adapters with membrane-tubulation activity that associates with transmembrane cargo proteins and initiates the formation of endocytic sites. Contributes to the stabilization of the nascent clathrin-coated pit. Plays also a role in late endocytosis by mediating vesiculation. Involved in the regulation of cell cycle-dependent dynamics of the septin cytoskeleton by promoting septin turnover in different cell cycle stages. May act through the RHO2 signaling pathway to repolarize cortical actin patches in profilin-deficient cells.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Internalization of diverse transmembrane cargos from the plasma membrane requires a similarly diverse array of specialized adaptors, yet only a few adaptors have been characterized. We report the identification of the muniscin family of endocytic adaptors that is conserved from yeast to human beings. Solving the structures of yeast muniscin domains confirmed the unique combination of an N-terminal domain homologous to the crescent-shaped membrane-tubulating EFC/F-BAR domains and a C-terminal domain homologous to cargo-binding mu homology domains (muHDs). In vitro and in vivo assays confirmed membrane-tubulation activity for muniscin EFC/F-BAR domains. The muHD domain has conserved interactions with the endocytic adaptor/scaffold Ede1/eps15, which influences muniscin localization. The transmembrane protein Mid2, earlier implicated in polarized Rho1 signalling, was identified as a cargo of the yeast adaptor protein. These and other data suggest a model in which the muniscins provide a combined adaptor/membrane-tubulation activity that is important for regulating endocytosis.

Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation.,Reider A, Barker SL, Mishra SK, Im YJ, Maldonado-Baez L, Hurley JH, Traub LM, Wendland B EMBO J. 2009 Oct 21;28(20):3103-16. Epub 2009 Aug 27. PMID:19713939^[5]

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

References

↑ Marcoux N, Cloutier S, Zakrzewska E, Charest PM, Bourbonnais Y, Pallotta D. Suppression of the profilin-deficient phenotype by the RHO2 signaling pathway in Saccharomyces cerevisiae. Genetics. 2000 Oct;156(2):579-92. PMID:11014808
↑ Qiu W, Neo SP, Yu X, Cai M. A novel septin-associated protein, Syp1p, is required for normal cell cycle-dependent septin cytoskeleton dynamics in yeast. Genetics. 2008 Nov;180(3):1445-57. doi: 10.1534/genetics.108.091900. Epub 2008, Sep 14. PMID:18791237 doi:http://dx.doi.org/10.1534/genetics.108.091900
↑ Reider A, Barker SL, Mishra SK, Im YJ, Maldonado-Baez L, Hurley JH, Traub LM, Wendland B. Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation. EMBO J. 2009 Oct 21;28(20):3103-16. Epub 2009 Aug 27. PMID:19713939 doi:10.1038/emboj.2009.248
↑ Stimpson HE, Toret CP, Cheng AT, Pauly BS, Drubin DG. Early-arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast. Mol Biol Cell. 2009 Nov;20(22):4640-51. Epub 2009 Sep 23. PMID:19776351 doi:http://dx.doi.org/E09-05-0429
↑ Reider A, Barker SL, Mishra SK, Im YJ, Maldonado-Baez L, Hurley JH, Traub LM, Wendland B. Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation. EMBO J. 2009 Oct 21;28(20):3103-16. Epub 2009 Aug 27. PMID:19713939 doi:10.1038/emboj.2009.248

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3g9g"

@@ Line 7: / Line 7: @@
 <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=3g9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3g9g RCSB], [http://www.ebi.ac.uk/pdbsum/3g9g PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/SYP1_YEAST SYP1_YEAST]] Multi-functional protein that contributes to the endocytic process, but also to events that occur at the neck during budding and/or cytokinesis. Plays a role as an endocytic adapters with membrane-tubulation activity that associates with transmembrane cargo proteins and initiates the formation of endocytic sites. Contributes to the stabilization of the nascent clathrin-coated pit. Plays also a role in late endocytosis by mediating vesiculation. Involved in the regulation of cell cycle-dependent dynamics of the septin cytoskeleton by promoting septin turnover in different cell cycle stages. May act through the RHO2 signaling pathway to repolarize cortical actin patches in profilin-deficient cells.<ref>PMID:11014808</ref> <ref>PMID:18791237</ref> <ref>PMID:19713939</ref> <ref>PMID:19776351</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3g9g

From Proteopedia

Revision as of 17:07, 25 December 2014

Crystal Structure of the N-terminal EFC/F-BAR domain of Syp1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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