PMID- 23970415
OWN - NLM
STAT- MEDLINE
DCOM- 20140425
LR  - 20211203
IS  - 1477-9137 (Electronic)
IS  - 0021-9533 (Print)
IS  - 0021-9533 (Linking)
VI  - 126
IP  - Pt 17
DP  - 2013 Sep 1
TI  - Syndecan-4 signaling at a glance.
PG  - 3799-804
LID - 10.1242/jcs.124636 [doi]
AB  - Syndecan-4, a ubiquitous cell surface proteoglycan, mediates numerous cellular 
      processes through signaling pathways that affect cellular proliferation, 
      migration, mechanotransduction and endocytosis. These effects are achieved 
      through syndecan-4 functioning as both a co-receptor for the fibroblast growth 
      factor receptors (FGFR1-FGFR4) and its ability to independently activate 
      signaling pathways upon ligand binding. As an FGFR co-receptor, syndecan-4 
      strengthens the duration and intensity of downstream signaling upon ligand 
      binding; this is particularly evident with regard to mitogen-activated protein 
      kinase (MAPK) signaling. In contrast, syndecan-4 also functions as an independent 
      receptor for heparin-binding growth factors, such as fibroblast growth factors 
      (FGFs), vascular endothelial growth factors (VEGFs) and platelet-derived growth 
      factors (PDGFs). These signaling cascades affect canonical signaling components, 
      such as the mammalian target of rapamycin (mTOR), AKT1 and the Rho family of 
      GTPases. In combination with the integrin family of proteins, syndecan-4 is also 
      able to form physical connections between the extracellular matrix (ECM) and 
      cytoskeletal signaling proteins, and it has a key role in regulation of integrin 
      turnover. This unique versatility of the interactions of syndecan-4 is 
      characterized in this Cell Science at a Glance article and illustrated in the 
      accompanying poster.
FAU - Elfenbein, Arye
AU  - Elfenbein A
AD  - Yale Cardiovascular Research Center, Section of Cardiovascular Medicine, 
      Department of Internal Medicine, Yale University, New Haven, CT 06520, USA.
FAU - Simons, Michael
AU  - Simons M
LA  - eng
GR  - R01 HL062289/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Review
DEP - 20130822
PL  - England
TA  - J Cell Sci
JT  - Journal of cell science
JID - 0052457
RN  - 0 (Platelet-Derived Growth Factor)
RN  - 0 (SDC4 protein, human)
RN  - 0 (Syndecan-4)
RN  - 0 (VEGFA protein, human)
RN  - 0 (Vascular Endothelial Growth Factor A)
RN  - 0 (platelet-derived growth factor A)
RN  - 62031-54-3 (Fibroblast Growth Factors)
RN  - EC 2.7.1.1 (MTOR protein, human)
RN  - EC 2.7.11.1 (AKT1 protein, human)
RN  - EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
RN  - EC 2.7.11.1 (TOR Serine-Threonine Kinases)
RN  - EC 3.6.5.2 (rho GTP-Binding Proteins)
SB  - IM
MH  - Cell Membrane/metabolism
MH  - *Cell Movement
MH  - *Cell Proliferation
MH  - *Endocytosis
MH  - Fibroblast Growth Factors/metabolism
MH  - Humans
MH  - *Mechanotransduction, Cellular
MH  - Platelet-Derived Growth Factor/metabolism
MH  - Proto-Oncogene Proteins c-akt/metabolism
MH  - Signal Transduction
MH  - Syndecan-4/*metabolism
MH  - TOR Serine-Threonine Kinases/metabolism
MH  - Vascular Endothelial Growth Factor A/metabolism
MH  - rho GTP-Binding Proteins/metabolism
PMC - PMC3757327
EDAT- 2013/08/24 06:00
MHDA- 2014/04/26 06:00
PMCR- 2014/09/01
CRDT- 2013/08/24 06:00
PHST- 2013/08/24 06:00 [entrez]
PHST- 2013/08/24 06:00 [pubmed]
PHST- 2014/04/26 06:00 [medline]
PHST- 2014/09/01 00:00 [pmc-release]
AID - jcs.124636 [pii]
AID - 10.1242/jcs.124636 [doi]
PST - ppublish
SO  - J Cell Sci. 2013 Sep 1;126(Pt 17):3799-804. doi: 10.1242/jcs.124636. Epub 2013 
      Aug 22.