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Literature summary for 3.1.4.39 extracted from

  • Fulkerson, Z.; Wu, T.; Sunkara, M.; Kooi, C.V.; Morris, A.J.; Smyth, S.S.
    Binding of autotaxin to integrins localizes lysophosphatidic acid production to platelets and mammalian cells (2011), J. Biol. Chem., 286, 34654-34663.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.4.39

Activating Compound

Activating Compound Comment Organism Structure
integrins ATX activity against exogenously provided and cell-associated substrates is increased by integrin binding Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Homo sapiens
-
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
blood
-
 Homo sapiens
-

Subunits

Subunits Comment Organism
monomer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
ATX
-
 Homo sapiens
autotaxin
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction ATX SMB2 mutants with impaired binding to beta3 integrins display reduced LPA generating capacity. Mutation of a charged, surface-exposed residue at the N-terminus of the ATX SMB2 domain significantly reduces binding of ATX to platelet integrins. The effects of ATX on platelet and cell-associated LPA production, but not hydrolysis of small molecule or detergent-solubilized substrates, are attenuated by point mutations in the SMB2 that impair integrin binding Homo sapiens
additional information ATX interacts with integrins, possible role for the solvent-exposed surface of the N-terminal tandem somatomedin B-like domains in binding to platelet integrin alphaIIbbeta3. The opposite face of the somatomedin B-like domain interacts with the catalytic phosphodiesterase domain to form a hydrophobic channel through which lysophospholipid substrates enter and leave the active site. Integrin binding therefore localizes ATX activity to the cell surface, providing a mechanism to generate LPA in the vicinity of its receptors Homo sapiens
physiological function ATX moderately facilitates platelet adhesion to fibrinogen, synergistic effect of platelet activation and ATX on LPA generation. ATX binding to platelet integrins enables agonist-stimulated LPA production. The lysophospholipase D generates the bioactive lipid mediator lysophosphatidic acid. Integrin-bound ATX can access cell surface substrates and deliver LPA to cell surface receptors Homo sapiens