Da. Deangelis et Pe. Braun, 2',3'-CYCLIC NUCLEOTIDE 3'-PHOSPHODIESTERASE BINDS TO ACTIN-BASED CYTOSKELETAL ELEMENTS IN AN ISOPRENYLATION-INDEPENDENT MANNER, Journal of neurochemistry, 67(3), 1996, pp. 943-951
2',3'-Cyclic nucleotide 3'-phosphodiesterase (CNP) is an isoprenylated
protein enriched in myelin and oligodendrocytes but also present in s
everal other tissues at low levels. CNP binds avidly to membranes and
in addition possesses several characteristics of cytoskeletal proteins
. The role of isoprenylation in the association of CNP with the cytosk
eleton was analyzed by ectopic expression in L cells of epitope-tagged
CNP1 and a non-isoprenylated mutant CNP1. Using nonionic detergent ex
traction, drug-mediated cytoskeletal disruption, and coimmunoprecipita
tion with an anti-actin antibody, we show that CNP1 is associated with
actin-based cytoskeletal elements independently of its isoprenylation
status. A control protein, p21c-H-ras, which is also modified by isop
renylation at its carboxyl-terminus, does not bind to cytoskeletal str
uctures as judged by the same criteria. We present a model that accoun
ts for the association of CNP1 with membranes and the cytoskeleton.