The cytoplasmic carboxy-terminal amino acid specifies cleavage of membrane TGFα into soluble growth factor Journal Article


Authors: Bosenberg, M. W.; Pandiella, A.; Massagué, J.
Article Title: The cytoplasmic carboxy-terminal amino acid specifies cleavage of membrane TGFα into soluble growth factor
Abstract: Membrane-anchored transforming growth factor α (proTGFα) belongs to a group of transmembrane proteins whose extracellular domains are selectively cleaved and released into the medium. We demonstrate that the carboxy-terminal valine in the cytoplasmic tail of proTGFα is required for cleavage of the growth factor ectodomain in response to various activators. This cleavage process occurs outside Golgi or lysosomal locations, affects cell surface proTGFα, and requires little or no membrane traffic. We propose that cleavage and release of proTGFα ectodomain involve a specialized proteolytic system and depend on the recognition of a simple and specific determinant located in the proTGFα cytoplasmic tail. © 1992 Cell Press.
Keywords: nonhuman; protein domain; animal cell; animal; carboxy terminal sequence; protein degradation; membrane proteins; animalia; amino acid sequence; molecular sequence data; cytoplasm; valine; transforming growth factor alpha; cho cell; cho cells; protein precursors; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.; support, u.s. gov't, non-p.h.s.; hamsters
Journal Title: Cell
Volume: 71
Issue: 7
ISSN: 0092-8674
Publisher: Cell Press  
Date Published: 1992-12-24
Start Page: 1157
End Page: 1165
Language: English
DOI: 10.1016/s0092-8674(05)80064-9
PUBMED: 1473151
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 30 July 2019 -- Source: Scopus
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  1. Joan Massague
    388 Massague