CLIP-170 links endocytic vesicles to microtubules.
Binding of endocytic carrier vesicles to microtubules depends on the microtubule-binding protein CLIP-170 in vitro. In vivo, CLIP-170 colocalizes with a subset of transferrin receptor-positive endocytic structures and, more extensively, with endosomal tubules induced by brefeldin A. The structure of CLIP-170 has been analyzed by cloning its cDNA. The predicted non-helical C- and N-terminal domains of the homodimeric protein are connected by a long coiled-coil domain. We have identified a novel motif present in a tandem repeat in the N-terminal domain of CLIP-170 that is involved in binding to microtubules. This motif is also found in the Drosophila Glued and yeast BIK1 proteins. These features, together with its very elongated structure, suggest that CLIP-170 belongs to a novel class of proteins, cytoplasmic linker proteins (CLIPs), mediating interactions of organelles with microtubules.
European Molecular Biology Laboratory, Heidelberg, Germany.
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P
Pierre
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Scheel
J E
JE
Rickard
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TE
Kreis
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004705:Endocytosis / Q000502:physiology; D011992:Endosomes / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D008870:Microtubules / Q000378:metabolism*; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins; D012689:Sequence Homology, Nucleic Acid
D008869:Microtubule-Associated Proteins; D009363:Neoplasm Proteins; C076744:cytoplasmic linker protein 170