The anatomy and cell biology of peripheral myelin protein-22.
The gain of function phenotypes exhibited by the heterozygous Tr, Tr-J, and CMT1A mutations indicate that these mutations interfere with more than the function of a single PMP22 allele. The identification of proteins that interact with PMP22 and that are sensitive both to stoichiometry and the effects of the mutations could provide important leads to a unified hypothesis to explain the riddle of the PMP22-related neuropathies.
Snipes
G J
GJ
Department of Neurology and Neurosurgery, McGill University, Montreal, Quebec, Canada. jsnipes@mni.lan.mcgill.ca
Orfali
W
W
Fraser
A
A
Dickson
K
K
Colby
J
J
D000818:Animals; D002607:Charcot-Marie-Tooth Disease / Q000235:genetics* / Q000503:physiopathology; D006801:Humans; D051379:Mice; D008818:Mice, Neurologic Mutants; D009185:Myelin Proteins / Q000235:genetics* / Q000502:physiology
D009185:Myelin Proteins; C073687:PMP22 protein, human; C489545:Pmp22 protein, mouse