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. 1990 Nov;10(11):6089–6090. doi: 10.1128/mcb.10.11.6089

Identification of a putative yeast homolog of the mammalian beta chains of the clathrin-associated protein complexes.

T Kirchhausen 1
PMCID: PMC361412  PMID: 2122239

Abstract

The clathrin-associated protein complexes are heterotetrameric structures believed to interact with clathrin and with membrane components of mammalian coated pits and coated vesicles. I have identified a yeast homolog of the mammalian beta-type large chains, suggesting the existence in yeast cells of clathrin-associated protein complexes. A sequence comparison between the putative yeast beta-type chain and its mammalian counterparts shows that their amino-terminal domains are related over their entire length and that their carboxyl-terminal domains diverge completely. This observation is consistent with our earlier proposal (T. Kurchhausen et al., Proc. Natl. Acad. Sci. USA 86:2612-2616, 1989) for the bifunctional-domain organization of the large chains, in which the invariant amino-terminal region interacts with conserved proteins of the coat while the variable carboxyl-terminal domain interacts with different membrane components of coated pits and coated vesicles.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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