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Article

Mutational analysis of betaCOP (Sec26p) identifies an appendage domain critical for function.

BMC cell biology - 22 Jan 2008

DeRegis Carol J, Rahl Peter B, Hoffman Gregory R, Cerione Richard A, Collins Ruth N

Abstract excerpt

BACKGROUND: The appendage domain of the gammaCOP subunit of the COPI vesicle coat bears a striking structural resemblance to adaptin-family appendages despite limited primary sequence homology. Both the gammaCOP appendage domain and an equivalent region on betaCOP contain the FxxxW motif; the conservation of this motif suggested the existence of a functional appendage domain in betaCOP. RESULTS: Sequence...

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Share to Coatomer Protein
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Fungal

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Share to GTPase-Activating Proteins

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Source

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Identifiers

PMID: 18211691
DOI: 10.1186/1471-2121-9-3
PMCID: PMC2262067

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Mutational analysis of betaCOP (Sec26p) identifies an appendage domain critical for function.PMID 18211691Read ↗

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