palmitoleoylation

{{short description|Biochemical reaction}}

{{distinguish|palmitoylation}}

File:Palmitoleic acid.svg, pictured above) is added.]]

Palmitoleoylation is type of protein lipidation where the monounsaturated fatty acid palmitoleic acid is covalently attached to serine or threonine residues of proteins.{{Cite journal|last=Hannoush|first=Rami N.|date=2015|title=Synthetic protein lipidation|journal=Current Opinion in Chemical Biology|volume=28|pages=39–46|doi=10.1016/j.cbpa.2015.05.025|issn=1879-0402|pmid=26080277}}{{Cite book|series=Advances in Experimental Medicine and Biology|title=Vertebrate Development : Maternal to Zygotic Control|date=2017|publisher=Springer International Publishing|editor1=Pelegri F|editor2=Danilchik M|editor3=Sutherland A|isbn=9783319460956|location=Cham|oclc=979974353}} Palmitoleoylation appears to play a significant role in trafficking and targeting and function of Wnt proteins.{{Cite journal|last=Hosseini|first=Vahid|last2=Dani|first2=Christian|last3=Geranmayeh|first3=Mohammad Hossein|last4=Mohammadzadeh|first4=Fatemeh|last5=Nazari Soltan Ahmad|first5=Saeed|last6=Darabi|first6=Masoud|date=2018-10-20|title=Wnt lipidation: Roles in trafficking, modulation, and function|journal=Journal of Cellular Physiology|volume=234|issue=6|pages=8040–8054|doi=10.1002/jcp.27570|issn=1097-4652|pmid=30341908}}{{Cite journal|last=Nile|first=Aaron H.|last2=Hannoush|first2=Rami N.|date=February 2016|title=Fatty acylation of Wnt proteins|journal=Nature Chemical Biology|volume=12|issue=2|pages=60–69|doi=10.1038/nchembio.2005|issn=1552-4469|pmid=26784846}}{{cite journal |vauthors=Takada R, Satomi Y, Kurata T, Ueno N, Norioka S, Kondoh H, Takao T, Takada S | title=Monounsaturated fatty acid modification of Wnt protein: its role in Wnt secretion | journal=Dev Cell | year=2006 | volume=11 | issue=6 | pages=791–801 | pmid= 17141155 | doi=10.1016/j.devcel.2006.10.003| doi-access=free }}

O-Palmitoleoylation of Wnt proteins is catalysed by PORCN. The inverse reaction is done by NOTUM.{{cite journal | doi = 10.1016/j.tibs.2017.04.004 | pmid = 28602500 | title = Dynamic Protein Acylation: New Substrates, Mechanisms, and Drug Targets | journal = Trends in Biochemical Sciences | volume = 42 | issue = 7 | pages = 566–581 | year = 2017 | last1 = Lanyon-Hogg | first1 = Thomas | last2 = Faronato | first2 = Monica | last3 = Serwa | first3 = Remigiusz A. | last4 = Tate | first4 = Edward W. | hdl = 10044/1/48121 | hdl-access = free }}