Ia. Wilson et al., DIFFERENTIAL LOCALIZATION OF THE MESSENGER-RNA OF THE M-ISOFORMS AND B-ISOFORMS OF CREATINE-KINASE IN MYOBLASTS, Biochemical journal, 308, 1995, pp. 599-605
Creatine kinase (CK) plays an important role in buffering ATP and ADP
levels in tissues which have intermittently high and fluctuating energ
y demands, such as skeletal muscle. This buffering function has a spat
ial, as well as a temporal aspect, which is dependent on the localizat
ion of different enzyme isoforms within the cell. We show here, by in
situ hybridization, that the mRNAs for the cytoplasmic isoforms of CK
are differentially localized in a mouse myoblast cell line (C2C12). Th
e mRNA for the M form is localized at the cell periphery, while that f
or the B form is localized in the perinuclear region. Deletion of segm
ents of the 3' untranslated regions of these mRNAs or swapping of thes
e segments between the mRNAs for the two isoforms demonstrated that lo
calization signals lie within these regions. Localization appears to b
e tissue-specific, since both the M and B mRNAs were distributed unifo
rmly over the cytoplasm in a non-muscle cell line. These results, in c
onjunction with other studies which have shown that mRNA localization
can lead to co-localization of the encoded protein, suggest that the l
ocalization of the mRNAs for the cytoplasmic isoforms of CK may be inv
olved in the localization of the enzymes themselves.