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1
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0030660196
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Syndecans: Multifunctional cell-surface co-receptors
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Carey DJ. Syndecans: multifunctional cell-surface co-receptors. Biochem J. 327:1997;1-16.
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(1997)
Biochem J
, vol.327
, pp. 1-16
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Carey, D.J.1
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2
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0032080892
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Syndecans: Synergistic activators of cell adhesion
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Woods A, Couchman JR. Syndecans: synergistic activators of cell adhesion. Trends Cell Biol. 8:1998;189-192.
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(1998)
Trends Cell Biol
, vol.8
, pp. 189-192
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Woods, A.1
Couchman, J.R.2
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3
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-
0030669701
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Structure - Activity relationship of heparan sulphate
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Gallagher JT. Structure - activity relationship of heparan sulphate. Biochem Soc Trans. 25:1997;1206-1209.
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(1997)
Biochem Soc Trans
, vol.25
, pp. 1206-1209
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Gallagher, J.T.1
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4
-
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0030775796
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Cell-surface heparan sulfate proteoglycans: Dynamic molecules mediating ligand catabolism
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of special interest. The internalization of proteoglycans, largely through catabolism of their glycosaminoglycan chains, has been documented previously. This paper addresses the determinants of the syndecan core protein necessary for its uptake and localization to internalization sites on the membrane
-
Williams KJ, Fuki IV. Cell-surface heparan sulfate proteoglycans: dynamic molecules mediating ligand catabolism. of special interest Curr Opin Lipidol. 8:1997;253-262 The internalization of proteoglycans, largely through catabolism of their glycosaminoglycan chains, has been documented previously. This paper addresses the determinants of the syndecan core protein necessary for its uptake and localization to internalization sites on the membrane.
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(1997)
Curr Opin Lipidol
, vol.8
, pp. 253-262
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Williams, K.J.1
Fuki, I.V.2
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5
-
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0030330635
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The glypican family of heparan sulfate proteoglycans: Major cell-surface proteoglycans of the developing nervous system
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Lander AD, Stipp CS, Ivins JK. The glypican family of heparan sulfate proteoglycans: major cell-surface proteoglycans of the developing nervous system. Perspect Dev Neurobiol. 3:1996;347-358.
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(1996)
Perspect Dev Neurobiol
, vol.3
, pp. 347-358
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Lander, A.D.1
Stipp, C.S.2
Ivins, J.K.3
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6
-
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0032514259
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Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells
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of outstanding interest. This work provides exciting evidence for the potential linkage of syndecans to the cytoskeleton and a means of anchorage at the basolateral surface of epithelial cells
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Cohen AR, Woods DF, Marfatia SM, Walther Z, Chishti AH, Anderson JM. Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells. of outstanding interest J Cell Biol. 142:1998;129-138 This work provides exciting evidence for the potential linkage of syndecans to the cytoskeleton and a means of anchorage at the basolateral surface of epithelial cells.
-
(1998)
J Cell Biol
, vol.142
, pp. 129-138
-
-
Cohen, A.R.1
Woods, D.F.2
Marfatia, S.M.3
Walther, Z.4
Chishti, A.H.5
Anderson, J.M.6
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7
-
-
0031457554
-
Syntenin, a PDZ protein that binds syndecan cytoplasmic domains
-
of outstanding interest. This is the first report of PDZ protein binding to syndecan cytoplasmic domains and suggests a mechanism for syndecan clustering and anchorage at the plasma membrane
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Grootjans JJ, Zimmermann P, Reekmans G, Smets A, Degeest G, Durr J, David G. Syntenin, a PDZ protein that binds syndecan cytoplasmic domains. of outstanding interest Proc Natl Acad Sci USA. 94:1997;13683-13688 This is the first report of PDZ protein binding to syndecan cytoplasmic domains and suggests a mechanism for syndecan clustering and anchorage at the plasma membrane.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 13683-13688
-
-
Grootjans, J.J.1
Zimmermann, P.2
Reekmans, G.3
Smets, A.4
Degeest, G.5
Durr, J.6
David, G.7
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8
-
-
0032514263
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Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
-
of outstanding interest. Another exciting report of CASK binding to syndecans, here, syndecan-2 in the synapse. The synapse is an excellent example of receptor clustering and anchorage to a highly organized membrane domain and may serve as a paradigm for syndecan anchorage in other types of cells
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Hsueh Y-P, Yang F-C, Kharazia V, Naisbitt S, Cohen AR, Weinberg RJ, Sheng M. Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses. of outstanding interest J Cell Biol. 142:1998;139-151 Another exciting report of CASK binding to syndecans, here, syndecan-2 in the synapse. The synapse is an excellent example of receptor clustering and anchorage to a highly organized membrane domain and may serve as a paradigm for syndecan anchorage in other types of cells.
-
(1998)
J Cell Biol
, vol.142
, pp. 139-151
-
-
Hsueh Y-P1
Yang F-C2
Kharazia, V.3
Naisbitt, S.4
Cohen, A.R.5
Weinberg, R.J.6
Sheng, M.7
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9
-
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0030889054
-
Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C
-
of outstanding interest. This paper, together with [10-12], documents the binding of activated PKCα to the syndecan-4 cytoplasmic domain. This pioneering work is the first clear evidence for intracellular signaling molecules binding directly to syndecans. The localization of syndecan-4 in focal adhesions makes it a central player in the signaling that occurs in these structures
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Oh ES, Woods A, Couchman JR. Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C. of outstanding interest J Biol Chem. 272:1997;8133-8136 This paper, together with [10-12], documents the binding of activated PKCα to the syndecan-4 cytoplasmic domain. This pioneering work is the first clear evidence for intracellular signaling molecules binding directly to syndecans. The localization of syndecan-4 in focal adhesions makes it a central player in the signaling that occurs in these structures.
-
(1997)
J Biol Chem
, vol.272
, pp. 8133-8136
-
-
Oh, E.S.1
Woods, A.2
Couchman, J.R.3
-
10
-
-
0030911243
-
Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C
-
of outstanding interest. See annotation to [9]
-
Oh ES, Woods A, Couchman JR. Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C. of outstanding interest J Biol Chem. 272:1997;11805-11811 See annotation to [9].
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(1997)
J Biol Chem
, vol.272
, pp. 11805-11811
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-
Oh, E.S.1
Woods, A.2
Couchman, J.R.3
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11
-
-
0032562706
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Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4,5-bisphosphate coordinately regulate protein kinase C activity
-
of outstanding interest. See annotation to [9]
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Oh ES, Woods A, Lim ST, Theibert AW, Couchman JR. Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4,5-bisphosphate coordinately regulate protein kinase C activity. of outstanding interest J Biol Chem. 273:1998;10624-10629 See annotation to [9].
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(1998)
J Biol Chem
, vol.273
, pp. 10624-10629
-
-
Oh, E.S.1
Woods, A.2
Lim, S.T.3
Theibert, A.W.4
Couchman, J.R.5
-
12
-
-
0032557438
-
Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4,5-bisphosphate
-
of outstanding interest. See annotation to [9]
-
Lee D, Oh ES, Woods A, Couchman JR, Lee W. Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4,5-bisphosphate. of outstanding interest J Biol Chem. 273:1998;13022-13029 See annotation to [9].
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(1998)
J Biol Chem
, vol.273
, pp. 13022-13029
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-
Lee, D.1
Oh, E.S.2
Woods, A.3
Couchman, J.R.4
Lee, W.5
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13
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0029953925
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Syndecans, signaling and cell adhesion
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Couchman JR, Woods A. Syndecans, signaling and cell adhesion. J Cell Biochem. 61:1996;578-584.
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(1996)
J Cell Biochem
, vol.61
, pp. 578-584
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Couchman, J.R.1
Woods, A.2
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14
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0028880289
-
Protein kinase C regulates the recruitment of syndecan-4 into focal contacts
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Baciu PC, Goetinck PF. Protein kinase C regulates the recruitment of syndecan-4 into focal contacts. Mol Biol Cell. 6:1995;1503-1513.
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(1995)
Mol Biol Cell
, vol.6
, pp. 1503-1513
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Baciu, P.C.1
Goetinck, P.F.2
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15
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0030960152
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Identification of an adhesion site within the syndecan-4 extracellular protein domain
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of special interest of outstanding interest. This paper, together with the following report [16], is the first work showing that syndecan extracellular protein domains have roles in molecular interactions apart from their heparan sulfate chains
-
McFall AJ, Rapraeger AC. Identification of an adhesion site within the syndecan-4 extracellular protein domain. of special interest of outstanding interest J Biol Chem. 272:1997;12901-12904 This paper, together with the following report [16], is the first work showing that syndecan extracellular protein domains have roles in molecular interactions apart from their heparan sulfate chains.
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(1997)
J Biol Chem
, vol.272
, pp. 12901-12904
-
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McFall, A.J.1
Rapraeger, A.C.2
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16
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0032561184
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Characterization of the high-affinity cell binding domain in the cell surface proteoglycan syndecan-4
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of outstanding interest of special interest
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McFall AJ, Rapraeger AC. Characterization of the high-affinity cell binding domain in the cell surface proteoglycan syndecan-4. of outstanding interest of special interest J Biol Chem. 1998; See annotation to [15].
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(1998)
J Biol Chem
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McFall, A.J.1
Rapraeger, A.C.2
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17
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0028842497
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Self-association of N-syndecan (syndecan-3) core protein is mediated by a novel structural motif in the transmembrane domain and ectodomain flanking region
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Asundi VK, Carey DJ. Self-association of N-syndecan (syndecan-3) core protein is mediated by a novel structural motif in the transmembrane domain and ectodomain flanking region. J Biol Chem. 270:1995;26404-26410.
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(1995)
J Biol Chem
, vol.270
, pp. 26404-26410
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Asundi, V.K.1
Carey, D.J.2
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18
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0027315260
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A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation
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Woods A, McCarthy JB, Furcht LT, Couchman JR. A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation. Mol Biol Cell. 4:1993;605-613.
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(1993)
Mol Biol Cell
, vol.4
, pp. 605-613
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Woods, A.1
McCarthy, J.B.2
Furcht, L.T.3
Couchman, J.R.4
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20
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0031749471
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Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2
-
of special interest. This and the following two reports [21,22] begin to look at the regulation and physiological significance of syndecan shedding. This places the shed ectodomains and their multifunctional heparan sulfate chains within wound sites where they are likely to be key regulators of wound healing processes
-
Kato M, Wang H, Kainulainen V, Fitzgerald ML, Ledbetter S, Omitz DM, Bernfield M. Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2. of special interest Nat Med. 4:1998;691-697 This and the following two reports [21,22] begin to look at the regulation and physiological significance of syndecan shedding. This places the shed ectodomains and their multifunctional heparan sulfate chains within wound sites where they are likely to be key regulators of wound healing processes.
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(1998)
Nat Med
, vol.4
, pp. 691-697
-
-
Kato, M.1
Wang, H.2
Kainulainen, V.3
Fitzgerald, M.L.4
Ledbetter, S.5
Omitz, D.M.6
Bernfield, M.7
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21
-
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0030967612
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Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth factor receptor activation
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of special interest. See annotation to [20]
-
Subramanian SV, Fitzgerald ML, Bernfield M. Regulated shedding of syndecan-1 and -4 ectodomains by thrombin and growth factor receptor activation. of special interest J Biol Chem. 272:1997;14713-14720 See annotation to [20].
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(1997)
J Biol Chem
, vol.272
, pp. 14713-14720
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Subramanian, S.V.1
Fitzgerald, M.L.2
Bernfield, M.3
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22
-
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0032496145
-
Syndecans, heparan sulfate proteoglycans, maintain the proteolytic balance of acute wound fluids
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of special interest. See annotation to [20]
-
Kainulainen V, Wang H, Schick C, Bernfield M. Syndecans, heparan sulfate proteoglycans, maintain the proteolytic balance of acute wound fluids. of special interest J Biol Chem. 273:1998;11563-11569 See annotation to [20].
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(1998)
J Biol Chem
, vol.273
, pp. 11563-11569
-
-
Kainulainen, V.1
Wang, H.2
Schick, C.3
Bernfield, M.4
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23
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0032575578
-
Heparan sulfate proteoglycans as adhesive and anti-invasive molecules: Syndecans and glypicans have distinct functions
-
of special interest. An interesting paper that extends the work from this group and begins to analyze the domains of syndecan-1 that influence signaling during cell invasion
-
Liu W, Litwack ED, Stanley MJ, Langford JK, Lander AD, Sanderson RA. Heparan sulfate proteoglycans as adhesive and anti-invasive molecules: syndecans and glypicans have distinct functions. of special interest J Biol Chem. 273:1998;22825-22832 An interesting paper that extends the work from this group and begins to analyze the domains of syndecan-1 that influence signaling during cell invasion.
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(1998)
J Biol Chem
, vol.273
, pp. 22825-22832
-
-
Liu, W.1
Litwack, E.D.2
Stanley, M.J.3
Langford, J.K.4
Lander, A.D.5
Sanderson, R.A.6
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24
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0030293766
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Protein - Protein interactions: PDZ domain networks
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Fanning AS, Anderson J. Protein - protein interactions: PDZ domain networks. Curr Biol. 6:1996;1385-1388.
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(1996)
Curr Biol
, vol.6
, pp. 1385-1388
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Fanning, A.S.1
Anderson, J.2
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25
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15644379801
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Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
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Songyang Z, Fanning AS, Fu C, Xu J, Marfatia SM, Chishti AH, Crompton A, Chan AC, Anderson JM, Cantley LC. Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science. 275:1997;73-77.
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(1997)
Science
, vol.275
, pp. 73-77
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Songyang, Z.1
Fanning, A.S.2
Fu, C.3
Xu, J.4
Marfatia, S.M.5
Chishti, A.H.6
Crompton, A.7
Chan, A.C.8
Anderson, J.M.9
Cantley, L.C.10
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26
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0029914941
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CASK: A novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins
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Hata Y, Butz S, Sudhof TC. CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins. J Neurosci. 16:1996;2488-2494.
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(1996)
J Neurosci
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, pp. 2488-2494
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Hata, Y.1
Butz, S.2
Sudhof, T.C.3
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27
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0030763609
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The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C. Analysis of the binding interface by in vitro mutagenesis
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Marfatia SM, Morais-Cabral JH, Kim AC, Byron O, Chishti AH. The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C. Analysis of the binding interface by in vitro mutagenesis. J Biol Chem. 272:1997;24191-24197.
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J Biol Chem
, vol.272
, pp. 24191-24197
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Marfatia, S.M.1
Morais-Cabral, J.H.2
Kim, A.C.3
Byron, O.4
Chishti, A.H.5
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28
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0029143156
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Tight junctions, membrane-associated guanylate kinases and cell signaling
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Kim SK. Tight junctions, membrane-associated guanylate kinases and cell signaling. Curr Opin Cell Biol. 7:1995;641-649.
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Curr Opin Cell Biol
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Kim, S.K.1
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29
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0028917977
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Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein
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Marfatia SM, Leu RA, Branton D, Chishti AH. Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein. J Biol Chem. 270:1995;715-719.
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J Biol Chem
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Marfatia, S.M.1
Leu, R.A.2
Branton, D.3
Chishti, A.H.4
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31
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0030800927
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The ezrin protein family: Membrane - Cytoskeleton interactions and disease associations
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Vaheri A, Carpen O, Heiska L, Helander TS, Jaaskelainen J, Majander-Nordenswan P, Sainio M, Timonen T, Turunen O. The ezrin protein family: membrane - cytoskeleton interactions and disease associations. Curr Opin Cell Biol. 9:1997;659-666.
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(1997)
Curr Opin Cell Biol
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, pp. 659-666
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Vaheri, A.1
Carpen, O.2
Heiska, L.3
Helander, T.S.4
Jaaskelainen, J.5
Majander-Nordenswan, P.6
Sainio, M.7
Timonen, T.8
Turunen, O.9
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33
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0030926546
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Deciphering the function of neurexins at cellular junctions
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Littleton JT, Bhat MA, Bellen HJ. Deciphering the function of neurexins at cellular junctions. J Cell Biol. 137:1997;793-796.
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J Cell Biol
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, pp. 793-796
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Littleton, J.T.1
Bhat, M.A.2
Bellen, H.J.3
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34
-
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0032562591
-
Cortactin-Src kinase signaling pathway is involved in N-syndecan-dependent neurite outgrowth
-
of outstanding interest. An important paper that is the first description of tyrosine kinases isolated from cell extracts through interaction with a syndecan cytoplasmic domain; furthermore, the activity of the kinase complex is regulated by extracellular ligands binding the heparan sulfate chains on the syndecans
-
Kinnunen T, Kaksonen M, Saarinen J, Kalkkinen N, Peng HB, Rauvala H. Cortactin-Src kinase signaling pathway is involved in N-syndecan-dependent neurite outgrowth. of outstanding interest J Biol Chem. 273:1998;10702-10708 An important paper that is the first description of tyrosine kinases isolated from cell extracts through interaction with a syndecan cytoplasmic domain; furthermore, the activity of the kinase complex is regulated by extracellular ligands binding the heparan sulfate chains on the syndecans.
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(1998)
J Biol Chem
, vol.273
, pp. 10702-10708
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Kinnunen, T.1
Kaksonen, M.2
Saarinen, J.3
Kalkkinen, N.4
Peng, H.B.5
Rauvala, H.6
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35
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0030905752
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HB-GAM (heparin-binding growth-associated molecule) and heparin-type glycans in the development and plasticity of neuron-target contacts
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Rauvala H, Peng HB. HB-GAM (heparin-binding growth-associated molecule) and heparin-type glycans in the development and plasticity of neuron-target contacts. Prog Neurobiol. 52:1997;127-144.
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(1997)
Prog Neurobiol
, vol.52
, pp. 127-144
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Rauvala, H.1
Peng, H.B.2
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36
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0031214383
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Serine phosphorylation of syndecan-2 proteoglycan cytoplasmic domain
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Oh ES, Couchman JR, Woods A. Serine phosphorylation of syndecan-2 proteoglycan cytoplasmic domain. Arch Biochem Biophys. 344:1997;67-74.
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(1997)
Arch Biochem Biophys
, vol.344
, pp. 67-74
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Oh, E.S.1
Couchman, J.R.2
Woods, A.3
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37
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0029550431
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Protein kinase C phosphorylates two of the four known syndecan cytoplasmic domains in vitro
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Prasthofer T, Ek B, Ekman P, Owens R, Höök M, Johansson S. Protein kinase C phosphorylates two of the four known syndecan cytoplasmic domains in vitro. Biochem Mol Biol Intern. 36:1995;793-802.
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Biochem Mol Biol Intern
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Prasthofer, T.1
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Ekman, P.3
Owens, R.4
Höök, M.5
Johansson, S.6
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38
-
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0029929433
-
Phosphorylation of a membrane-intercalated proteoglycan, syndecan-2, expressed in a stroma-inducing clone from a mouse Lewis lung carcinoma
-
Itano N, Oguri K, Nagayasu Y, Kusano Y, Nakanishi H, David G, Okayama M. Phosphorylation of a membrane-intercalated proteoglycan, syndecan-2, expressed in a stroma-inducing clone from a mouse Lewis lung carcinoma. Biochem J. 315:1996;925-930.
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Biochem J
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, pp. 925-930
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Itano, N.1
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Kusano, Y.4
Nakanishi, H.5
David, G.6
Okayama, M.7
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39
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-
0032080332
-
Regulation of syndecan-4 phosphorylation in vivo
-
of special interest. An important paper that is one of the first descriptions of endogenous syndecan phosphorylation on serine. Importantly, it also shows regulation by FGF-2, a potential ligand for the syndecan
-
Horowitz A, Simons M. Regulation of syndecan-4 phosphorylation in vivo. of special interest J Biol Chem. 273:1998;10914-10918 An important paper that is one of the first descriptions of endogenous syndecan phosphorylation on serine. Importantly, it also shows regulation by FGF-2, a potential ligand for the syndecan.
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(1998)
J Biol Chem
, vol.273
, pp. 10914-10918
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Horowitz, A.1
Simons, M.2
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40
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17544378558
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The cytoplasmic domain of syndecan-1 is required for cytoskeleton association but not detergent insolubility. Identification of essential cytoplasmic domain residues
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Carey DJ, Bendt KM, Stahl RC. The cytoplasmic domain of syndecan-1 is required for cytoskeleton association but not detergent insolubility. Identification of essential cytoplasmic domain residues. J Biol Chem. 271:1996;15253-15260.
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(1996)
J Biol Chem
, vol.271
, pp. 15253-15260
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Carey, D.J.1
Bendt, K.M.2
Stahl, R.C.3
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41
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0031960011
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Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition
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Daniels DL, Cohen AR, Anderson JM, Brunger AT. Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition. Nat Struct Biol. 5:1998;317-325.
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(1998)
Nat Struct Biol
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Daniels, D.L.1
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Anderson, J.M.3
Brunger, A.T.4
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42
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0029853095
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Pervanadate activation of intracellular kinases leads to tyrosine phosphorylation and shedding of syndecan-1
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Reiland J, Ott VL, Lebakken CS, Yeaman C, McCarthy J, Rapraeger AC. Pervanadate activation of intracellular kinases leads to tyrosine phosphorylation and shedding of syndecan-1. Biochem J. 319:1996;39-47.
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Biochem J
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Reiland, J.1
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43
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Phosphorylation of recombinant N-syndecan (syndecan 3) core protein
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Asundi VK, Carey DJ. Phosphorylation of recombinant N-syndecan (syndecan 3) core protein. Biochem Biophys Res Commun. 240:1997;502-506.
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Asundi, V.K.1
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Syndecan-1 mediates cell spreading in transfected human lymphoblastoid (Rajl) cells
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Lebakken CS, Rapraeger AC. Syndecan-1 mediates cell spreading in transfected human lymphoblastoid (Rajl) cells. J Cell Biol. 132:1996;1209-1221.
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(1996)
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