Structural basis for Rab GTPase recognition and endosome tethering by the C₂H₂ zinc finger of Early...
Structural basis for Rab GTPase recognition and endosome tethering by the C₂H₂ zinc finger of Early Endosomal Autoantigen 1 (EEA1)
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United States: National Academy of Sciences
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Language
English
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United States: National Academy of Sciences
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Contents
Regulation of endosomal trafficking by Rab GTPases depends on selective interactions with multivalent effectors, including EEA1 and Rabenosyn-5, which facilitate endosome tethering, sorting, and fusion. Both EEA1 and Rabenosyn-5 contain a distinctive N-terminal C₂H₂ zinc finger that binds Rab5. How these C₂H₂ zinc fingers recognize Rab GTPases rema...
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Full title
Structural basis for Rab GTPase recognition and endosome tethering by the C₂H₂ zinc finger of Early Endosomal Autoantigen 1 (EEA1)
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TN_cdi_fao_agris_US201301856423
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_fao_agris_US201301856423
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ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1000843107
