Identification of a putative yeast homolog of the mammalian beta chains of the clathrin-associated protein complexes.
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.
Kirchhausen
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Department of Anatomy and Cellular Biology, Harvard Medical School, Boston, Massachusetts 02115.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002966:Clathrin / Q000235:genetics*; D003034:Coated Pits, Cell-Membrane / Q000378:metabolism; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes; D051381:Rats; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid
D002966:Clathrin; D046911:Macromolecular Substances; D015345:Oligonucleotide Probes