PMP22 exon 4 deletion causes ER retention of PMP22 and a gain-of-function allele in CMT1E

Ann Clin Transl Neurol. 2017 Mar 12;4(4):236-245. doi: 10.1002/acn3.395. eCollection 2017 Apr.

Abstract

Objective: To determine whether predicted fork stalling and template switching (FoSTeS) during mitosis deletes exon 4 in peripheral myelin protein 22 KD (PMP22) and causes gain-of-function mutation associated with peripheral neuropathy in a family with Charcot-Marie-Tooth disease type 1E.

Methods: Two siblings previously reported to have genomic rearrangements predicted to involve exon 4 of PMP22 were evaluated clinically and by electrophysiology. Skin biopsies from the proband were studied by RT-PCR to determine the effects of the exon 4 rearrangements on exon 4 mRNA expression in myelinating Schwann cells. Transient transfection studies with wild-type and mutant PMP22 were performed in Cos7 and RT4 cells to determine the fate of the resultant mutant protein.

Results: Both affected siblings had a sensorimotor dysmyelinating neuropathy with severely slow nerve conduction velocities (<10 m/sec). RT-PCR studies of Schwann cell RNA from one of the siblings demonstrated a complete in-frame deletion of PMP22 exon 4 (PMP22Δ4). Transfection studies demonstrated that PMP22Δ4 protein is retained within the endoplasmic reticulum and not transported to the plasma membrane.

Conclusions: Our results confirm that that FoSTeS-mediated genomic rearrangement produced a deletion of exon 4 of PMP22, resulting in expression of both PMP22 mRNA and protein lacking this sequence. In addition, we provide experimental evidence for endoplasmic reticulum retention of the mutant protein suggesting a gain-of-function mutational mechanism consistent with the observed CMT1E in this family. PMP22Δ4 is another example of a mutated myelin protein that is misfolded and contributes to the pathogenesis of the neuropathy.