Identification of a 48‐kDa prenylated protein that associates with microtubules as 2′,3′‐cyclic nucleotide 3′‐phosphodiesterase in FRTL‐5 cells

Farnesyltransferase inhibitors induce dramatic morphological changes of KNRK cells that are blocked by microtubule interfering agents

“…It may be the case that farnesylated proteins associate with microtubules and directly affect their regulation. In this regard, it is interesting to note that cyclic nucleotide phosphodiesterase (CNPase) (21,22) has been reported to be associated with microtubules (35). There are two isoforms of CNPase, CNP1 (46 kDa) and CNP2 (48 kDa), and both contain the C-terminal CysThrIleIle sequence.…”

Pharmacological Actions of Statins: A Critical Appraisal in the Management of Cancer

“…In the case of prelamin A, there is an additional farnesylationdependent endoproteolysis, which is defective in two congenital diseases: Hutchinson-Gilford progeria and restrictive dermopathy (Young at al., 2006). Finally, one of the earliest myelin-related proteins expressed when OLGs differentiate, 2Ј,3Ј-cyclic-nucleotide-3Јphospho-diesterase is farnesylated and palmitoylated and is involved in the regulation of cytoarchitecture through its interaction with microtubules and microfilaments (Braun et al, 1991;Laezza et al, 1997;Bifulco et al, 2002).…”

v-K- ras leads to preferential farnesylation of p21 ras in FRTL-5 cells: Multiple interference with the isoprenoid pathway

“…Densitometric analysis of the major prenylated proteins in Ats cells in experiments was performed at different times after p21 ras activation, so as to characterize the kinetics of the K-ras-induced changes in the protein prenylation profile, and revealed a different time-dependent disappearance of prenylation for the 48-and 21-to 25-kDa proteins. In fact, the former protein, previously identified as 2Ј, 3Ј-cyclic nucleotide 3Ј-phosphodiesterase (CNP) (22), disap- (Fig. 1 A).…”

“…Cells then were washed three times with ice-cold PBS, were scraped from the dish, and were lysed in hypotonic buffer. Equal amounts of each protein extract (Ϸ100 g) were analyzed by 12% SDS͞ PAGE as described (20)(21)(22).…”