2 PDZ DOMAIN PROTEINS ENCODED BY THE MURINE PERIAXIN GENE ARE THE RESULT OF ALTERNATIVE INTRON RETENTION AND ARE DIFFERENTIALLY TARGETED INSCHWANN-CELLS
L. Dytrych et al., 2 PDZ DOMAIN PROTEINS ENCODED BY THE MURINE PERIAXIN GENE ARE THE RESULT OF ALTERNATIVE INTRON RETENTION AND ARE DIFFERENTIALLY TARGETED INSCHWANN-CELLS, The Journal of biological chemistry, 273(10), 1998, pp. 5794-5800
Periaxin was first described as a 147-kDa protein that was suggested t
o have a potential role in the initiation of myelin deposition in peri
pheral nerves based upon its abundance, cell type specificity, pattern
of developmental expression, and localization (Gillespie, C. S., Sher
man, D. L., Blair, G. E., and Brophy. P. J. (1994) Neuron 12, 497-508)
, Here we show that the murine periaxin gene spans 20.6 kilobases and
encodes two mRNAs of 4.6 and 5.2 kilobases that encode two periaxin is
oforms, L-periaxin and S-periaxin of 147 and 16 kDa respectively. The
larger mRNA is produced by a retained intron mechanism that introduces
a stop codon and results in a truncated protein with an intron-encode
d C terminus of 21 amino acids. Both proteins possess a PDZ domain at
the N terminus; nevertheless, they are targeted differently in Schwann
cells, Like other proteins that contain PDZ domains, L-periaxin is lo
calized to the plasma membrane of myelinating Schwann cells: in contra
st, S-periaxin is expressed diffusely in the cytoplasm, This suggests
that proteins that contain this protein-binding module may also partic
ipate in protein-protein interactions at sites other than the cell cor
tex.