A novel intracellular fibulin-1D variant binds to the cytoplasmic domain of integrin beta 1 subunit.

ABSTRACT: Fibulin-1 is a member of a growing family of proteins that includes eight members and is involved in cellular functions such as adhesion, migration and differentiation. Fibulin-1 has also been implicated in embryonic development of the heart and neural crest-derived structures. It is an integral part of the extracellular matrix (ECM) and has been shown to bind to a multitude of ECM proteins. However, fibulin-1 was first identified as a protein purified from placental extracts that binds to the cytoplasmic domain of integrin β1. Human fibulin-1 is alternatively spliced into four different isoforms namely A-D. These isoforms share a common N-terminus sequence that contains a secretion sequence but differ in their carboxy-terminal fibulin-1 module. In this report we identify a new splice vari

SUBMITTER: Twal WO 

PROVIDER: S-EPMC4446149 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature