AI Article Synopsis
- Many proteins undergo post-translational modifications by lipid groups like palmitoyl or farnesyl, forming functional proteolipids.
- These lipid modifications increase a protein's hydrophobic characteristics, promoting its attachment to cell membranes.
- A key example is the farnesylation of the Ras GTPase, which is crucial for directing this signaling protein to the plasma membrane.
Article Abstract
Many proteins are post-translationally modified by lipid moieties such as palmitoyl or prenyl (e.g., farnesyl) groups, creating functional proteolipids. Lipid modifications share the property of increasing a protein's hydrophobicity and thus the propensity of that protein to associate with a membrane. These modifications are used to control the localization and activity of membrane-associated proteins. A well-recognized paradigm is farnesylation of the Ras GTPase that helps target this critical signaling protein to the plasma membrane.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3414401 | PMC |
| http://dx.doi.org/10.4161/nucl.20391 | DOI Listing |
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