PMID: 9164866May 15, 1997Paper

Identification of the cleavage sites in the alpha6A integrin subunit: structural requirements for cleavage and functional analysis of the uncleaved alpha6Abeta1 integrin

The Biochemical Journal
G O DelwelA Sonnenberg

Abstract

The alpha6A and alpha6B integrin subunits are proteolytically cleaved during biosynthesis into a heavy chain (120 kDa) that is disulphide-linked to one of two light chains (31 or 30 kDa). Analysis of the structure of the alpha6A subunit on the carcinoma cell line T24 and human platelets demonstrated that the two light chains of alpha6 are not differentially glycosylated products of one polypeptide. Rather they possess different polypeptide backbones, which presumably result from proteolytic cleavage at distinct sites in the alpha6 precursor. Mutations were introduced in the codons for the R876KKR879, E883K884, R890K891 and R898K899 sequences, the potential proteolytic cleavage sites, and wild-type and mutant alpha6A cDNAs were transfected into K562 cells. The mutant alpha6A integrin subunits were expressed in association with endogenous beta1 at levels comparable to that of wild-type alpha6Abeta1. A single alpha6 polypeptide chain (150 kDa) was precipitated from transfectants expressing alpha6A with mutations or deletions in the RKKR sequence. Mutations in the EK sequence yielded alpha6A subunits that were cleaved once into a heavy and a light chain, whereas alpha6A subunits with mutations in one of the two RK sequences were, l...Continue Reading

Citations

May 22, 2001·The Journal of Biological Chemistry·T L DavisA E Cress
Nov 2, 2012·The Journal of Clinical Investigation·Nayia NicolaouArnoud Sonnenberg
Jul 13, 2007·Immunological Reviews·Ana Kasirer-FriedeSanford J Shattil
Mar 10, 2005·Virchows Archiv : an International Journal of Pathology·Philipp StawowyKristof Graf
Dec 18, 2007·Biochemical and Biophysical Research Communications·Manolis C DemetriouParis Skourides

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