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. 2013 May 20;23(10):R431-5.
doi: 10.1016/j.cub.2013.04.024.

Covalent lipid modifications of proteins

Marilyn D Resh  1
Affiliations

Covalent lipid modifications of proteins

Marilyn D Resh. Curr Biol. .
No abstract available

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Figures

Figure 1
Figure 1. Localization and regulation of lipid modified proteins
Conceptual diagram of representative proteins modified with various lipophilic groups. Lipid rafts (blue bilayer) are enriched in GPI-anchored proteins (green) on the outer leaflet, and palmitoylated proteins (blue) on the inner leaflet. GPI-anchored proteins can be released from the cell by phospholipases. Depalmitoylation by palmitoyl thioesterases (PTEs) releases palmitoylated proteins from the cytoplasmic side of the membrane. N-myristoylated proteins (red) can undergo a myristoyl switch and dissociate from the membrane. H-Ras, a protein modified with farnesyl and palmitate (purple), localizes to both the plasma membrane and the Golgi. H-Ras can be released from the plasma membrane by depalmitoylation, rebind to the Golgi, where it is repalmitoylated, and then undergo vesicular trafficking back to the plasma membrane. Geranylgeranylated proteins (light purple) can be extracted from the bilayer by the action of GDIs. A secreted protein that is lipid modified is represented by Hh (yellow). Hh is modified by palmitate and cholesterol in the ER, traffics through the secretory pathway, and is released from the cell.
See this image and copyright information in PMC

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