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- W1840600420 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." @default.
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- W1840600420 date "1990-11-01" @default.
- W1840600420 modified "2023-10-18" @default.
- W1840600420 title "Identification of a putative yeast homolog of the mammalian beta chains of the clathrin-associated protein complexes." @default.
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- W1840600420 doi "https://doi.org/10.1128/mcb.10.11.6089" @default.
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