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Farnesyltransferase, CAAX box, alpha

Prenyltransferases can attach either a farnesyl group or a geranylgeranyl group in thioether linkage to the cysteine residue of proteins with a C-terminal CAAX box. CAAX geranylgeranyltransferase and CAAX farnesyltransferase are heterodimers that share the same alpha subunit but have different beta subunits. This gene encodes the alpha subunit of these transferases. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 11 and 13. [provided by RefSeq, May 2010] (from NCBI)
Papers on FNTA
Geranylgeranyl transferase 1 modulates autophagy and apoptosis in human airway smooth muscle.
Halayko et al., Winnipeg, Canada. In Am J Physiol Lung Cell Mol Physiol, 2012
our findings identify Geranylgeranyl transferase 1 as a key regulator of human airway smooth muscle cell viability
The protein farnesyltransferase regulates HDAC6 activity in a microtubule-dependent manner.
Giannakakou et al., Atlanta, United States. In J Biol Chem, 2009
FTase, via its tubulin-association, is a critical upstream regulator of HDAC6 activity
Dominant-negative alpha-subunit of farnesyl- and geranyltransferase inhibits glucose-stimulated, but not KCl-stimulated, insulin secretion in INS 832/13 cells.
Kowluru et al., Detroit, United States. In Diabetes, 2007
Geranylgeranyltransferase inhibitor-2147 (GGTI-2147), an inhibitor of protein prenylation, elicited significant inhibition of glucose-stimulated insulin secretion from INS 832/13 islet cells.
Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity.
Beese et al., Durham, United States. In J Mol Biol, 2004
Results suggest that all peptide substrates adopt a common binding mode in the protein farnesyltransferase and geranylgeranyltransferase active site.
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