4hmy

From Proteopedia

(Difference between revisions)

Revision as of 12:03, 25 December 2014

Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1

Structural highlights

4hmy is a 5 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	Adtg, Ap1g1, Clapg1 (Mus musculus), ADTB1, AP1B1, BAM22, CLAPB2 (Homo sapiens), Ap1m1, Cltnm (Mus musculus), AP1S3 (Homo sapiens), ARF1 (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[AP1G1_MOUSE] Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. [AP1M1_MOUSE] Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. [ARF1_HUMAN] GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles.

Publication Abstract from PubMed

AP-1 is a clathrin adaptor complex that sorts cargo between the trans-Golgi network and endosomes. AP-1 recruitment to these compartments requires Arf1-GTP. The crystal structure of the tetrameric core of AP-1 in complex with Arf1-GTP, together with biochemical analyses, shows that Arf1 activates cargo binding by unlocking AP-1. Unlocking is driven by two molecules of Arf1 that bridge two copies of AP-1 at two interaction sites. The GTP-dependent switch I and II regions of Arf1 bind to the N terminus of the beta1 subunit of one AP-1 complex, while the back side of Arf1 binds to the central part of the gamma subunit trunk of a second AP-1 complex. A third Arf1 interaction site near the N terminus of the gamma subunit is important for recruitment, but not activation. These observations lead to a model for the recruitment and activation of AP-1 by Arf1.

Structural Basis for Recruitment and Activation of the AP-1 Clathrin Adaptor Complex by Arf1.,Ren X, Farias GG, Canagarajah BJ, Bonifacino JS, Hurley JH Cell. 2013 Feb 14;152(4):755-67. doi: 10.1016/j.cell.2012.12.042. PMID:23415225^[1]

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

References

↑ Ren X, Farias GG, Canagarajah BJ, Bonifacino JS, Hurley JH. Structural Basis for Recruitment and Activation of the AP-1 Clathrin Adaptor Complex by Arf1. Cell. 2013 Feb 14;152(4):755-67. doi: 10.1016/j.cell.2012.12.042. PMID:23415225 doi:http://dx.doi.org/10.1016/j.cell.2012.12.042

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4hmy"

@@ 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=4hmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hmy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hmy RCSB], [http://www.ebi.ac.uk/pdbsum/4hmy PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/AP1G1_MOUSE AP1G1_MOUSE]] Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. [[http://www.uniprot.org/uniprot/AP1M1_MOUSE AP1M1_MOUSE]] Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. [[http://www.uniprot.org/uniprot/ARF1_HUMAN ARF1_HUMAN]] GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4hmy

From Proteopedia

Revision as of 12:03, 25 December 2014

Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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