Geranylgeranylation
The geranylgeranylation (falsely shortened Geranylierung ) is a form of prenylation of proteins .
properties
Geranylgeranylation is a post-translational modification of proteins through which, among other things, cytosolic proteins are attached to the cell membrane or to other biomembranes in a cell via the attached geranylgeranyl group in the sense of a membrane anchor . The substrates in geranylgeranylation are geranyl pyrophosphate and one or two C -terminal cysteines on the protein to be modified. The leaving group in geranylgeranylation is pyrophosphate .
Two enzymes bring about geranylgeranylation, geranylgeranyltransferase I (GGTase I) or Rab-GGTase (synonym GGTase II). GGTase I modifies cysteines in the C -terminal amino acid sequence CXXL, similar to the farnesyltransferases in farnesylation . GGTase II modifies two cysteines each with a geranylgeranyl group in the sequence CXC or XXCC, the proteins to be modified are then transported to the membrane by the protein REP ( rab escort factor ).
Examples of geranylgeranylated proteins are e.g. B. the Rho-GTPase and the γ-subunit of heterotrimeric G-proteins .
literature
- EM Storck, RA Serwa, EW Tate: Chemical proteomics: a powerful tool for exploring protein lipidation. In: Biochemical Society Transactions . Volume 41, number 1, February 2013, pp. 56-61, doi : 10.1042 / BST20120283 , PMID 23356258 .
Individual evidence
- ^ KF Leung, R. Baron, MC Seabra: Thematic review series: lipid posttranslational modifications. geranylgeranylation of Rab GTPases. In: Journal of Lipid Research . Volume 47, Number 3, March 2006, pp. 467-475, doi : 10.1194 / jlr.R500017-JLR200 , PMID 16401880 .
- ↑ S. Yalovsky: Protein lipid modifications and the regulation of ROP GTPase function. In: Journal of Experimental Botany . Volume 66, Number 6, March 2015, pp. 1617–1624, doi : 10.1093 / jxb / erv057 , PMID 25711710 .