A superfamily of membrane-bound O-acyltransferases with implications for wnt signaling.

By Kay Hofmann. 2000

503 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology

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Citations in the corpus

Wnt proteins are lipid-modified and can act as stem cell growth factors (2003, background): “have homology with acyl transferases and may catalyse Wnt acylatio”
Structural model of PORCN illuminates disease-associated variants and drug binding sites (2021, background): “PORCN is a member of the family of membrane-bound O-acyltransferases (MBOATs) (Hofmann, 2000), and catalyzes the transfer of an monounsaturated 16:1 palmitoleate from Coenzyme A, S-(9Z)-9-hexadecenoate (PAM-CoA) to the hydroxyl of the serine residue (see model, Figure 1A) (Heuvel et al.”
Structural basis for catalysis and substrate specificity of human ACAT1 (2020, background): “membrane-bound O-acyltransferase (MBOAT) family (4).”
Precise Regulation of Porcupine Activity Is Required for Physiological Wnt Signaling (2012, background): “Additionally, PORCN is most closely related to acyltransferases that act on lysophospholipid species (52) and was originally suggested to not modify Wnt directly but rather an associated sugar due to this homology (24).”
Structure, mechanism, and inhibition of Hedgehog acyltransferase (2021, background): “…defined a common architecture, sharing an 8-transmembrane (TM) helix core domain that contains the active site, including a conserved histidine (Hofmann, 2000) and in the case of the lipid-substrate MBOATs, acyl-coenzyme A:cholesterol acyltransferase 1 (ACAT) and…”
Stearoyl CoA desaturase is required to produce active, lipid-modified Wnt proteins (2013, background): “Porcn is a member of the membrane-bound O-acyltransferase (MBOAT) family (Hofmann, 2000) and is predicted to modify all Wnt family members containing the conserved Ser 209 equivalent (Takada et al.”
Thematic review series: Lipid Posttranslational Modifications. Protein palmitoylation by a family of DHHC protein S-acyltransferases Published, JLR Papers in Press, April 1, 2006. (2006, background): “sequence homology with O-acyltransferases (17) but lack the DHHC domain that is found in PATs.”
A Continuum of Anionic Charge: Structures and Functions of d-Alanyl-Teichoic Acids in Gram-Positive Bacteria (2003, background): “Comparison of DltB with a variety of O-acyltransferases identified two conserved motifs that may also link this transport protein to a superfamily of membrane-bound O-acyltransferases (219).”