Syndecan-4 and focal adhesion function

Current Opinion in Cell Biology

Volumn 13, Issue 5, 2001, Pages 578-583

  Woods, Anne ^a   Couchman, John R ^b  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^b IMPERIAL COLLEGE SCHOOL OF MEDICINE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CORE PROTEIN; GLYCOSAMINOGLYCAN; GUANOSINE TRIPHOSPHATASE; INTEGRIN; PROTEOGLYCAN; RHO FACTOR; SYNDECAN;

ANGIOGENESIS; CELL ADHESION; CELL DIFFERENTIATION; CELL MIGRATION; CELL VIABILITY; DATA ANALYSIS; FIBROBLAST; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; REVIEW; SIGNAL TRANSDUCTION; WOUND HEALING;

ANIMALIA;

EID: 0035479818     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(00)00254-4     Document Type: Review

References (57)

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2. The molecular architecture of focal adhesions
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4. In vivo co-distribution of fibronectin and actin fibers in granulation tissue: Immunofluorescence and electron microscope studies of the fibronexus at the myofibroblast surface
5. Integrin signaling and cell growth control
6. Bidirectional signaling between the cytoskeleton and integrins
7. Genetic analysis of β1 integrin function: Confirmed, new and revised roles for a crucial family of cell adhesion molecules
8. Syndecans and cell adhesion
9. Elucidation of the structural features of heparan sulfate important for interaction with the Hep-2 domain of fibronectin
10. Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts
11. Syndecan-4 signals cooperatively with integrins in a Rho-dependent manner in the assembly of focal adhesions and actin stress fibers
12. Functions of cell surface heparan sulfate proteoglycans
13. Syndecans: Multifunctional cell-surface co-receptors
14. The syndecans, tuners of transmembrane signaling
15. Syndecan-regulated receptor signaling
16. Molecular biology of ryudocan, an endothelial heparan sulfate proteoglycan
17. Syndecan 4 heparan sulfate proteoglycan is a selectively enriched and widespread focal adhesion component
18. Control of morphology, cytoskeleton and migration by syndecan-4
19. Protein-protein interactions: PDZ domain networks
20. Syntenin, a PDZ protein that binds syndecan cytoplasmic domains
21. Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
22. Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration
23. Characterization of syntenin, a syndecan-binding PDZ protein, as a component of cell adhesion sites and microfilaments
24. Cell surface heparan sulfate proteoglycan syndecan-2 induces the maturation of dendritic spines in rat hippocampal neurons
25. Synbindin, a novel syndecan-2-binding protein in neuronal dendritic spines
26. Identification of syntenin as a protein of the apical early endocytic compartment in Madin-Darby canine kidney cells
27. A PDZ protein regulates the distribution of the transmembrane semaphoring, M-SemF
28. Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN
29. Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C
30. Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C
31. Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4,5-bisphosphate coordinately regulate protein kinase C activity
32. Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4,5-bisphosphate
33. Syndesmos, a protein that interacts with the cytoplasmic domain of syndecan-4, mediates cell spreading and actin cytoskeletal organization
34. Regulation of syndecan-4 phosphorylation in vivo
35. Phosphorylation of the cytoplasmic tail of syndecan-4 regulates activation of protein kinase Cα
36. Phosphatidylinositol-4,5-bisphosphate mediates the interaction of syndecan-4 with protein kinase C
37. Syntenin-syndecan binding requires syndecan-synteny and the cooperation of both PDZ domains of syntenin
38. Syndecan-4 core protein is sufficient for the assembly of focal adhesions and stress fibers
39. Heparan sulfate chains from glypican and syndecans bind the Hep II domain of fibronectin similarly despite minor structural differences
40. The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to β1 integrin-dependent cell spreading
41. Rho GTPases and their effector proteins
42. Dissection of pathways implicated in integrin-mediated actin cytoskeleton assembly. Involvement of protein kinase C, Rho GTPase, and tyrosine phosphorylation
43. Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover
44. Ezrin links syndecan-2 to the cytoskeleton
45. Cortactin-Src kinase signaling pathway is involved in N-syndecan-dependent neurite outgrowth
46. Syndecan-4 associations with the microfilament cytoskeleton and integrins
47. Rat embryo fibroblasts require both cell- and heparin-binding domains of fibronectin for survival
48. Syndecan-1 and -4 are induced during wound repair of neonatal but not fetal skin
49. Myocyte-dependent regulation of endothelial cell syndecan-4 expression: Role of TNF-α
50. Syndecan-4 is a primary-response gene induced by basic fibroblast growth factor and arterial injury in vascular smooth muscle cells
51. Syndecan-4 deficiency impairs focal adhesion formation only under restricted conditions
52. Delayed wound repair and impaired angiogenesis in mice lacking syndecan-4
53. Syndecan-4 deficiency impairs the fetal vessels in the placental labyrinth
54. Syndecan-4 deficiency increases susceptibility to kappa-carrageenan-induced renal damage
55. Shedding of syndecan-1 and -4 ectodomains is regulated by multiple signaling pathways and mediated by a TIMP-3-sensitive metalloproteinase
56. Plasma levels of syndecan-4 (ryudocan) are elevated in patients with acute myocardial infarction
57. Syndecan-4 up-regulation in proliferative renal disease is related to microfilament organization