High-resolution analysis and functional mapping of cleavage sites and substrate proteins of furin in the human proteome.

ABSTRACT:

Background

There is a growing appreciation of the role of proteolytic processes in human health and disease, but tools for analysis of such processes on a proteome-wide scale are limited. Furin is a ubiquitous proprotein convertase that cleaves after basic residues and transforms secretory proproteins into biologically active proteins. Despite this important role, many furin substrates remain unknown in the human proteome.

Methodology/principal findings

We devised an approach for proteinase target identification that combines an in silico discovery pipeline with highly multiplexed proteinase activity assays. We performed in silico analysis of the human proteome and identified over 1,050 secretory proteins as potential furin substrates. We then used a multiplexed protease ass

SUBMITTER: Shiryaev SA 

PROVIDER: S-EPMC3545927 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature