کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10929617 | 1093275 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Fatty acylation and prenylation of proteins: what's hot in fat
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیولوژی سلول
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چکیده انگلیسی
Post-translational modification by covalent attachment of lipid groups helps proteins to associate with membranes, both intra- and extracellularly. The enzymology of protein S-acylation with fatty acids has been a stumbling block, but three pathways for this modification have now been identified in eukaryotes. It is not yet clear whether this reaction is enzymatic or facilitated by a chaperone-like mechanism. Work with Ras proteins has shown that an S-acylation/deacylation cycle, in cooperation with prenylation and carboxyl-methylation, may regulate their cycling between intracellular membrane compartments and subdomains, hence controlling their signalling activity. The two types of prenyl group, geranylgeranyl and farnesyl, themselves have surprisingly specific targeting roles for Ras superfamily members.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Current Opinion in Cell Biology - Volume 17, Issue 2, April 2005, Pages 190-196
Journal: Current Opinion in Cell Biology - Volume 17, Issue 2, April 2005, Pages 190-196
نویسندگان
Tony Magee, Miguel C Seabra,