1987
DOI: 10.1038/326154a0
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Clathrin light chains contain brain-specific insertion sequences and a region of homology with intermediate filaments

Abstract: The primary structures of four bovine clathrin light chains have been determined. Light chains LCa and LCb are homologous proteins encoded by different genes. In the brain the messenger RNA from these genes undergoes differential splicing to yield proteins having centrally inserted brain-specific sequences. A potentially alpha-helical region of the clathrin light chains shows homology with intermediate filament proteins.

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Cited by 135 publications
(108 citation statements)
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“…Clathrin-coated vesicles from this recycling process that have been isolated from mammalian brain are the principal source of material for most biochemical and structural analyses. The presence of brain-specific isoforms of clathrin light chains (Jackson et al 1987;Kirchhausen et al 1987), auxilin (Umeda et al 2000), dynamin (Urrutia et al 1997), AP180 (Bushlin et al 2008), and various other proteins of the presynaptic membrane-recycling pathway may reflect features of the clathrin cycle in synapses that are not shared with classical, receptor-mediated endocytosis as studied in epithelial cells and fibroblasts.…”
Section: Clathrin-requiring Pathways Of Ligand Uptake the Canonical Pmentioning
confidence: 99%
“…Clathrin-coated vesicles from this recycling process that have been isolated from mammalian brain are the principal source of material for most biochemical and structural analyses. The presence of brain-specific isoforms of clathrin light chains (Jackson et al 1987;Kirchhausen et al 1987), auxilin (Umeda et al 2000), dynamin (Urrutia et al 1997), AP180 (Bushlin et al 2008), and various other proteins of the presynaptic membrane-recycling pathway may reflect features of the clathrin cycle in synapses that are not shared with classical, receptor-mediated endocytosis as studied in epithelial cells and fibroblasts.…”
Section: Clathrin-requiring Pathways Of Ligand Uptake the Canonical Pmentioning
confidence: 99%
“…1) and incorrectly large molecular masses indicated by electrophoretic mobilities in SDS-PAGE ( [9] and estimation for brain CLb of 25.1 kDa [12] to be 29 and 32 kDa in Fig. 1).…”
Section: Clb Purified From Post-mt Supernatant Potently Inhibitsmentioning
confidence: 89%
“…Since the 29-kDa protein was seen in the purified CLb but not its crude preparations (see Fig. 3), it is likely to be a proteolytic product of brain CLb and not non-(severely)-proteolyzed non-brain CLb (23.1 kDa [12]). …”
Section: Clb Purified From Post-mt Supernatant Potently Inhibitsmentioning
confidence: 97%
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“…CK II phosphorylates preferentially acidic amino acid sequences of type SEEE: serine followed by a cluster of acidic amino acids such as glutamic acid [22]. The complete amino acid sequence of the P-light chain of clathrin from brain and lymphocytes has been recently determined [23]. Moreover, the amino acid sequence of exposed region of the P-light chain has been also determined in native triskelions and CVs [24].…”
Section: In Vivo Phosphorylationmentioning
confidence: 99%