NuMA is a protein involved in maintenance of nuclear structure and in
the assembly of the mitotic spindle. Expression of amino-terminal dele
tion mutants results in a phenotype identical to that caused by a temp
erature-sensitive defect of RCC1 (regulator of chromosome condensation
). Here we describe the isolation of NuMA protein from HeLa cells unde
r mild conditions as a prerequisite to study its interactions with ele
ments of the RCC1-Ran regulatory pathway. In an overlay assay, NuMA di
d not bind Ran.[gamma-P-32]GTP. Thus it is clearly different from Ran.
GTP binding proteins of similar M(1).