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Research Article

Biosynthesis of the v-sis gene product: signal sequence cleavage, glycosylation, and proteolytic processing.

M Hannink, D J Donoghue
M Hannink
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D J Donoghue
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DOI: 10.1128/MCB.6.4.1343
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ABSTRACT

The v-sis oncogene and its cellular homolog c-sis encode chain B of platelet-derived growth factor. Cells transformed by v-sis produce a platelet-derived growth factor-related molecule which is able to stimulate the platelet-derived growth factor receptor in an autocrine fashion. Site-directed mutagenesis was used to construct several mutations which substitute charged residues for hydrophobic residues in the proposed signal sequence of the v-sis gene product. Two of these mutations resulted in the synthesis of altered v-sis gene products with an unexpected nuclear location and a loss of biological activity. We also report here the intracellular localization of the v-sis gene product to the endoplasmic reticulum-Golgi compartment, where signal sequence cleavage and N-linked glycosylation occur. The v-sis gene product contains no transmembrane regions, as it is completely protected within isolated microsomes from trypsin proteolysis. Site-directed mutagenesis was also used to alter a proposed proteolytic processing site in the v-sis gene product. This mutant v-sis gene, which encodes Asn-Ser in place of Lys-Arg at residues 110 to 111, was found to retain full biological activity.

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Biosynthesis of the v-sis gene product: signal sequence cleavage, glycosylation, and proteolytic processing.
M Hannink, D J Donoghue
Molecular and Cellular Biology Apr 1986, 6 (4) 1343-1348; DOI: 10.1128/MCB.6.4.1343

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Biosynthesis of the v-sis gene product: signal sequence cleavage, glycosylation, and proteolytic processing.
M Hannink, D J Donoghue
Molecular and Cellular Biology Apr 1986, 6 (4) 1343-1348; DOI: 10.1128/MCB.6.4.1343
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