Proteolipid: Difference between revisions
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{{short description|Protein covalently bonded to lipids}} |
{{short description|Protein covalently bonded to lipids}} |
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{{distinguish|Lipoprotein}} |
{{distinguish|Lipoprotein}} |
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{{merge with|Lipid-anchored protein|date=July 2019}} |
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A '''proteolipid''' is a [[protein]] covalently linked to [[lipid]] molecules, which can be [[fatty acid]]s or [[sterol]]s. The process of such a linkage is known as '''protein lipidation''', and falls into the wider category of [[acylation]]. Proteolipids are abundant in brain tissue, and are also present in many other animal and plant tissues. They are proteins covalenently bound to fatty acid chains,<ref name="MeSH">{{cite web|title=MeSH Browser|url=https://meshb.nlm.nih.gov/record/ui?name=Proteolipids|website=meshb.nlm.nih.gov|access-date=11 March 2018|language=en}}</ref> granting them an interface for interacting with [[biological membrane]]s.<ref name="lipidhome"/> They are not to be confused with [[lipoproteins]], a kind of spherical assemblies made up of many molecules of lipids and some [[apolipoprotein]]s. |
A '''proteolipid''' is a [[protein]] covalently linked to [[lipid]] molecules, which can be [[fatty acid]]s or [[sterol]]s. The process of such a linkage is known as '''protein lipidation''', and falls into the wider category of [[acylation]]. Proteolipids are abundant in brain tissue, and are also present in many other animal and plant tissues. They are proteins covalenently bound to fatty acid chains,<ref name="MeSH">{{cite web|title=MeSH Browser|url=https://meshb.nlm.nih.gov/record/ui?name=Proteolipids|website=meshb.nlm.nih.gov|access-date=11 March 2018|language=en}}</ref> granting them an interface for interacting with [[biological membrane]]s.<ref name="lipidhome"/> They are not to be confused with [[lipoproteins]], a kind of spherical assemblies made up of many molecules of lipids and some [[apolipoprotein]]s. |
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Revision as of 14:09, 19 July 2019
A proteolipid is a protein covalently linked to lipid molecules, which can be fatty acids or sterols. The process of such a linkage is known as protein lipidation, and falls into the wider category of acylation. Proteolipids are abundant in brain tissue, and are also present in many other animal and plant tissues. They are proteins covalenently bound to fatty acid chains,[1] granting them an interface for interacting with biological membranes.[2] They are not to be confused with lipoproteins, a kind of spherical assemblies made up of many molecules of lipids and some apolipoproteins.
Depending on the type of fatty acid attached to the protein, a proteolipid can contain myristoyl, palmitoyl, or prenyl groups. These groups each serve different functions and have different preferences as to which amino acid residue they attach to. The processes are respectively named myristoylation (usually at N-terminal Gly), palmitoylation (to cysteine), and prenylation (also to cysteine). Despite the seemingly specific names, N-myristoylation and S-palmitoylation can also involve some other fatty acids, most commonly in plants and viral proteolipids.[2][3]
There exist some rarer forms of protein acylation, including serine O-octanoylation in ghrelin, serine O-palmitolation in Wnt proteins, and O-palmitoleoylation in histone H4 with LPCAT1. Hedgehog proteins are double-modified by (N-) palmitate and cholesterol. Some skin ceramides are proteolipids.[2] The amino group on lysine can also be myristoylation via a poorly-understood mechanism.[4]
See also
References
- ^ "MeSH Browser". meshb.nlm.nih.gov. Retrieved 11 March 2018.
- ^ a b c "Proteolipids - proteins modified by covalent attachment to lipids - N-myristoylated, S-palmitoylated, prenylated proteins, ghrelin, hedgehog proteins,". www.lipidhome.co.uk. Retrieved 18 July 2019.
- ^ Li, Y; Qi, B (2017). "Progress toward Understanding Protein S-acylation: Prospective in Plants". Frontiers in plant science. 8: 346. doi:10.3389/fpls.2017.00346. PMC 5364179. PMID 28392791.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ "Dynamic Protein Acylation: New Substrates, Mechanisms, and Drug Targets". Trends in Biochemical Sciences. 42 (7): 566–581. June 1, 2017. doi:10.1016/j.tibs.2017.04.004.
{{cite journal}}: Unknown parameter|authors=ignored (help)
External links
- Proteolipids at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- GO:0006497: gene ontology term for protein lipidation