Syndecan-4 binds Actn1

Stable Identifier
R-RNO-2750176
Type
Reaction [binding]
Species
Rattus norvegicus
Compartment
General
SVG |   | PPTX  | SBGN
Syndecan-4 binds Actn1

Syndecans have attached heparan sulfate (HS) and to a lesser extent chondroitin sulfate (CS) chains. These allow interactions with a large number of proteins. Various enzymes involved in post-translational HS chain modifications produce unique binding motifs that selectively recognize different proteins (Tkachenko et al. 2005). Syndecan-null mice have subtle phenotypes when compared with mice deficient in HS chain synthesis or modification (Echtermeyer et al. 2001, Ishiquro et al. 2001, Götte et al. 2002). GPI-anchored glypicans and matrix HSPGs such as perlecan may compensate for the absence of syndecans.

Syndecans are also signalling molecules, interacting with cytoplasmic proteins. Most of the work done has involved syndecan-4 (Multhaupt et al. 2009). The V-region of syndecan-4 interacts with the actin-bundling protein alpha-actinin (Greene et al. 2003, Choi et al. 2008, Shin et al. 2012), a direct link to the cell cytoskeleton.

Literature References
PubMed ID Title Journal Year
18621433 The oligomeric status of syndecan-4 regulates syndecan-4 interaction with alpha-actinin

Choi, Y, Kim, S, Lee, J, Ko, SG, Lee, W, Han, IO, Woods, A, Oh, ES

Eur. J. Cell Biol. 2008
Participants
Orthologous Events
Authored
Reviewed
Created