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| [[Image:2caz.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2caz| PDB=2caz | SCENE= }} | | {{STRUCTURE_2caz| PDB=2caz | SCENE= }} |
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| '''ESCRT-I CORE'''
| | ===ESCRT-I CORE=== |
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| ==Overview==
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| ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. Currently, the picture regarding assembly of ESCRTs on endosomes is incomplete. The structure of the conserved heterotrimeric ESCRT-I core presented here shows a fan-like arrangement of three helical hairpins, each corresponding to a different subunit. Vps23/Tsg101 is the central hairpin sandwiched between the other subunits, explaining the critical role of its "steadiness box" in the stability of ESCRT-I. We show that yeast ESCRT-I links directly to ESCRT-II, through a tight interaction of Vps28 (ESCRT-I) with the yeast-specific zinc-finger insertion within the GLUE domain of Vps36 (ESCRT-II). The crystal structure of the GLUE domain missing this insertion reveals it is a split PH domain, with a noncanonical lipid binding pocket that binds PtdIns3P. The simultaneous and reinforcing interactions of ESCRT-II GLUE domain with membranes, ESCRT-I, and ubiquitin are critical for ubiquitinated cargo progression from early to late endosomes.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16615893}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16615893 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16615893}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Vps36]] | | [[Category: Vps36]] |
| [[Category: Vps37]] | | [[Category: Vps37]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:36:50 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:05:21 2008'' |