Clathrin and adaptors

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Clathrin Adaptors Really Adapt

The clathrin pathway is the principal route for receptor-mediated endocytosis and growth factor downregulation. Heterotetrameric clathrin adaptors directly link the clathrin coat with cargo transmembrane proteins that are sorted into coated pits and vesicles. A paper in this issue of Cell describes the atomic structure of the adaptor-protein 2 (AP-2) core, the portion that makes contacts with t...

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Adaptors for clathrin-mediated traffic.

Clathrin-based systems are responsible for a large portion of vesicular traffic originating from the plasma membrane and the trans-Golgi network that reaches the endosomal compartment. The assembly of cytosolic clathrin forms the scaffold required for the local deformation of the membrane and for the formation of coated pits and vesicles. In this process, clathrin interacts in a coordinated fas...

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Identification of clathrin and clathrin adaptors on tubulovesicles of gastric acid secretory (oxyntic) cells.

γ-Adaptin and clathrin heavy chain were identified on tubulovesicles of gastric oxyntic cells with the anti-γ-adaptin monoclonal antibody (MAb) 100/3 and an anti-clathrin heavy chain MAb (MAb 23), respectively. In Western blots, crude gastric microsomes from rabbit and rat and density gradient-purified, H-K-ATPase-rich microsomes from these same species were immunoreactive for γ-adaptin and cla...

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AP-4, a novel protein complex related to clathrin adaptors.

Here we report the identification and characterization of AP-4, a novel protein complex related to the heterotetrameric AP-1, AP-2, and AP-3 adaptors that mediate protein sorting in the endocytic and late secretory pathways. The key to the identification of this complex was the cloning and sequencing of two widely expressed, mammalian cDNAs encoding new homologs of the adaptor beta and sigma su...

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In vivo phosphorylation of adaptors regulates their interaction with clathrin

The coat proteins of clathrin-coated vesicles (CCV) spontaneously self-assemble in vitro, but, in vivo, their self-assembly must be regulated. To determine whether phosphorylation might influence coat formation in the cell, the in vivo phosphorylation state of CCV coat proteins was analyzed. Individual components of the CCV coat were isolated by immunoprecipitation from Madin-Darby bovine kidne...

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ژورنال

عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

سال: 1998

ISSN: 0167-4889

DOI: 10.1016/s0167-4889(98)00056-1