KEGG   PATHWAY: myb04512
Entry
myb04512                    Pathway                                
Name
ECM-receptor interaction - Myotis brandtii (Brandt's bat)
Description
The extracellular matrix (ECM) consists of a complex mixture of structural and functional macromolecules and serves an important role in tissue and organ morphogenesis and in the maintenance of cell and tissue structure and function. Specific interactions between cells and the ECM are mediated by transmembrane molecules, mainly integrins and perhaps also proteoglycans, CD36, or other cell-surface-associated components. These interactions lead to a direct or indirect control of cellular activities such as adhesion, migration, differentiation, proliferation, and apoptosis. In addition, integrins function as mechanoreceptors and provide a force-transmitting physical link between the ECM and the cytoskeleton. Integrins are a family of glycosylated, heterodimeric transmembrane adhesion receptors that consist of noncovalently bound alpha- and beta-subunits.
Class
Environmental Information Processing; Signaling molecules and interaction
Pathway map
myb04512  ECM-receptor interaction
myb04512

Other DBs
GO: 0005201
Organism
Myotis brandtii (Brandt's bat) [GN:myb]
Gene
102238647  FREM2; FRAS1 related extracellular matrix protein 2 [KO:K23380]
102238707  SV2C; synaptic vesicle glycoprotein 2C [KO:K06258]
102238961  GP1BA; glycoprotein Ib platelet alpha subunit [KO:K06261]
102240493  LAMC1; laminin subunit gamma 1 [KO:K05635]
102241192  HSPG2; heparan sulfate proteoglycan 2 [KO:K06255]
102241364  DSPP; dentin sialophosphoprotein [KO:K23573]
102241550  CHAD; chondroadherin [KO:K06248]
102242014  ITGB3; integrin subunit beta 3 [KO:K06493]
102242274  NPNT; nephronectin [KO:K06824]
102242389  THBS2; thrombospondin 2 [KO:K04659]
102242641  COL4A6; collagen type IV alpha 6 chain [KO:K06237]
102242832  ITGA11; integrin subunit alpha 11 [KO:K06587]
102243536  COL4A2; collagen type IV alpha 2 chain [KO:K06237]
102243552  COL9A2; collagen type IX alpha 2 chain [KO:K08131]
102244301  LAMA4; laminin subunit alpha 4 [KO:K06241]
102244336  ITGA2; integrin subunit alpha 2 [KO:K06481]
102244635  ITGA1; integrin subunit alpha 1 [KO:K06480]
102244665  VTN; vitronectin [KO:K06251]
102244892  FN1; fibronectin 1 [KO:K05717]
102245069  [KO:K06266]
102245416  TNR; tenascin R [KO:K06252]
102245715  ITGA3; integrin subunit alpha 3 [KO:K06482]
102245794  SPP1; secreted phosphoprotein 1 [KO:K06250]
102245872  COL6A2; collagen type VI alpha 2 chain [KO:K06238]
102246007  DAG1; dystroglycan 1 [KO:K06265]
102246230  SV2A; synaptic vesicle glycoprotein 2A [KO:K06258]
102246659  ITGB8; integrin subunit beta 8 [KO:K06591]
102246966  GP6; glycoprotein VI platelet [KO:K06264]
102248184  THBS4; thrombospondin 4 [KO:K04659]
102248306  [KO:K06585]
102248314  COL4A3; collagen type IV alpha 3 chain [KO:K06237]
102248658  VWF; von Willebrand factor [KO:K03900]
102248763  [KO:K19719]
102248944  HMMR; hyaluronan mediated motility receptor [KO:K06267]
102249275  ITGB6; integrin subunit beta 6 [KO:K06589]
102249405  COL4A4; collagen type IV alpha 4 chain [KO:K06237]
102249508  COL4A1; collagen type IV alpha 1 chain [KO:K06237]
102249761  ITGA7; integrin subunit alpha 7 [KO:K06583]
102249821  GP9; glycoprotein IX platelet [KO:K06263]
102249845  COMP; cartilage oligomeric matrix protein [KO:K04659]
102250634  THBS3; thrombospondin 3 [KO:K04659]
102250973  LAMB1; laminin subunit beta 1 [KO:K05636]
102250983  THBS1; thrombospondin 1 [KO:K16857]
102251267  COL6A1; collagen type VI alpha 1 chain [KO:K06238]
102251306  COL9A3; collagen type IX alpha 3 chain [KO:K08131]
102251547  LAMB4; laminin subunit beta 4 [KO:K06245]
102251734  SV2B; synaptic vesicle glycoprotein 2B [KO:K06258]
102251791  CD44; CD44 molecule (Indian blood group) [KO:K06256]
102251821  SDC4; syndecan 4 [KO:K16338]
102251828  SDC1; syndecan 1 [KO:K06257]
102252550  TNC; tenascin C [KO:K06252]
102252569  RELN; reelin [KO:K06249] [EC:3.4.21.-]
102252761  ITGA2B; integrin subunit alpha 2b [KO:K06476]
102253526  ITGA8; integrin subunit alpha 8 [KO:K06584]
102253855  TNXB; tenascin XB [KO:K06252]
102253918  COL1A2; collagen type I alpha 2 chain [KO:K06236]
102254069  [KO:K06236]
102254080  COL6A6; collagen type VI alpha 6 chain [KO:K06238]
102254720  COL2A1; collagen type II alpha 1 chain [KO:K19719]
102255410  LAMA3; laminin subunit alpha 3 [KO:K06240]
102255770  COL6A5; collagen type VI alpha 5 chain [KO:K06238]
102255900  ITGA5; integrin subunit alpha 5 [KO:K06484]
102256058  LAMC3; laminin subunit gamma 3 [KO:K06247]
102256069  [KO:K06238]
102256125  CD47; CD47 molecule [KO:K06266]
102256202  LAMA1; laminin subunit alpha 1 [KO:K05637]
102256358  LAMC2; laminin subunit gamma 2 [KO:K06246]
102256410  MEPE; matrix extracellular phosphoglycoprotein [KO:K26442]
102256520  [KO:K06240]
102256779  COL4A5; collagen type IV alpha 5 chain [KO:K06237]
102256918  IBSP; integrin binding sialoprotein [KO:K06253]
102257218  DMP1; dentin matrix acidic phosphoprotein 1 [KO:K23328]
102257482  CD36; CD36 molecule [KO:K06259]
102257789  COL6A3; collagen type VI alpha 3 chain [KO:K06238]
102257827  GP5; glycoprotein V platelet [KO:K06260]
102258028  [KO:K06590]
102258165  LAMB3; laminin subunit beta 3 [KO:K06244]
102258333  [KO:K06590]
102258809  LAMB2; laminin subunit beta 2 [KO:K06243]
102258848  COL9A1; collagen type IX alpha 1 chain [KO:K08131]
102259547  ITGA4; integrin subunit alpha 4 [KO:K06483]
102259707  COL1A1; collagen type I alpha 1 chain [KO:K06236]
102260193  ITGA10; integrin subunit alpha 10 [KO:K06586]
102260390  ITGB4; integrin subunit beta 4 [KO:K06525]
102260401  ITGAV; integrin subunit alpha V [KO:K06487]
102260652  [KO:K06266]
102260978  ITGB1; integrin subunit beta 1 [KO:K05719]
102261192  TNN; tenascin N [KO:K06252]
102261526  LAMA2; laminin subunit alpha 2 [KO:K05637]
102261784  FREM1; FRAS1 related extracellular matrix 1 [KO:K23380]
102261916  ITGA6; integrin subunit alpha 6 [KO:K06485]
102262191  ITGB5; integrin subunit beta 5 [KO:K06588]
102263146  FRAS1; Fraser extracellular matrix complex subunit 1 [KO:K23379]
102263709  LAMA5; laminin subunit alpha 5 [KO:K06240]
Compound
G10505  Hyaluronic acid
Reference
  Authors
van der Flier A, Sonnenberg A.
  Title
Function and interactions of integrins.
  Journal
Cell Tissue Res 305:285-98 (2001)
DOI:10.1007/s004410100417
Reference
  Authors
Reddy KV, Mangale SS.
  Title
Integrin receptors: the dynamic modulators of endometrial function.
  Journal
Tissue Cell 35:260-73 (2003)
DOI:10.1016/S0040-8166(03)00039-9
Reference
  Authors
Milner R, Campbell IL.
  Title
The integrin family of cell adhesion molecules has multiple functions within the CNS.
  Journal
J Neurosci Res 69:286-91 (2002)
DOI:10.1002/jnr.10321
Reference
  Authors
Cichy J, Pure E.
  Title
The liberation of CD44.
  Journal
J Cell Biol 161:839-43 (2003)
DOI:10.1083/jcb.200302098
Reference
PMID:7698997
  Authors
Elenius K, Jalkanen M.
  Title
Function of the syndecans--a family of cell surface proteoglycans.
  Journal
J Cell Sci 107 ( Pt 11):2975-82 (1994)
Reference
  Authors
Son YJ, Scranton TW, Sunderland WJ, Baek SJ, Miner JH, Sanes JR, Carlson SS.
  Title
The synaptic vesicle protein SV2 is complexed with an alpha5-containing laminin on the nerve terminal surface.
  Journal
J Biol Chem 275:451-60 (2000)
DOI:10.1074/jbc.275.1.451
Reference
  Authors
Sid B, Sartelet H, Bellon G, El Btaouri H, Rath G, Delorme N, Haye B, Martiny L.
  Title
Thrombospondin 1: a multifunctional protein implicated in the regulation of tumor growth.
  Journal
Crit Rev Oncol Hematol 49:245-58 (2004)
DOI:10.1016/j.critrevonc.2003.09.009
Reference
  Authors
Canobbio I, Balduini C, Torti M.
  Title
Signalling through the platelet glycoprotein Ib-V-IX complex.
  Journal
Cell Signal 16:1329-44 (2004)
DOI:10.1016/j.cellsig.2004.05.008
Reference
  Authors
Nieswandt B, Brakebusch C, Bergmeier W, Schulte V, Bouvard D, Mokhtari-Nejad R, Lindhout T, Heemskerk JW, Zirngibl H, Fassler R.
  Title
Glycoprotein VI but not alpha2beta1 integrin is essential for platelet interaction with collagen.
  Journal
EMBO J 20:2120-30 (2001)
DOI:10.1093/emboj/20.9.2120
Reference
  Authors
Martin PT.
  Title
Dystroglycan glycosylation and its role in matrix binding in skeletal muscle.
  Journal
Glycobiology 13:55R-66R (2003)
DOI:10.1093/glycob/cwg076
Reference
  Authors
Toole BP.
  Title
Hyaluronan: from extracellular glue to pericellular cue.
  Journal
Nat Rev Cancer 4:528-39 (2004)
DOI:10.1038/nrc1391
Reference
  Authors
Bosman FT, Stamenkovic I.
  Title
Functional structure and composition of the extracellular matrix.
  Journal
J Pathol 200:423-8 (2003)
DOI:10.1002/path.1437
Reference
  Authors
van der Ven AT, Vivante A, Hildebrandt F
  Title
Novel Insights into the Pathogenesis of Monogenic Congenital Anomalies of the Kidney and Urinary Tract.
  Journal
J Am Soc Nephrol 29:36-50 (2018)
DOI:10.1681/ASN.2017050561
Related
pathway
myb04510  Focal adhesion
KO pathway
ko04512   

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