Proprotein cleavage of E-cadherin by furin in baculovirus over-expression system: potential role of other convertases in mammalian cells.
Sequence analysis of the adhesion molecule E-cadherin had revealed a multibasic motif [4PArg-Gln-Lys-Arg1P], reminiscent of the minimal cleavage signal for furin, the prototype of the proprotein convertase family, and/or other members sharing similar sequence specificity. Mutation of this site was sufficient to abolish processing of E-cadherin in fibroblasts reinforcing the possibility that proprotein convertases are involved in the maturation of this adhesion molecule. Here we demonstrate that even though furin can efficiently and specifically cleave proE-cadherin in a baculovirus-based co-expression system, the furin-deficient LoVo cells were found to process endogenous E-cadherin as efficiently as normal cell lines. This suggests, for the first time, that E-cadherin is not only a substrate for furin but for other mammalian convertases sharing similar sequence specificity.
Posthaus
H
H
Institute of Animal Pathology, University of Bern, Switzerland.
Dubois
C M
CM
Laprise
M H
MH
Grondin
F
F
Suter
M M
MM
Müller
E
E
D000595:Amino Acid Sequence; D000818:Animals; D016367:Baculoviridae; D015820:Cadherins / Q000096:biosynthesis* / Q000737:chemistry / Q000378:metabolism; D002478:Cells, Cultured; D045683:Furin; D006801:Humans; D007313:Insecta; D007739:L Cells; D051379:Mice; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013381:Subtilisins / Q000378:metabolism*; D014162:Transfection
D015820:Cadherins; D021382:Protein Sorting Signals; D011994:Recombinant Proteins; D013381:Subtilisins; D045683:Furin