| Literature DB >> 26945032 |
Takuya Yagi1, Daisuke Ito2, Norihiro Suzuki2.
Abstract
The tropomyosin-receptor kinase fused gene(TFG), which is located on chromosome 3q12.2, was originally identified as a fusion partner that results in the formation of oncogenic products associated with multiple cancers. TFG protein interacts directly with Sec16, the scaffolding protein for coat protein II-coated vesicles that regulate endoplasmic reticulum (ER)-to-Golgi transport at ER exit sites. In 2012, a heterozygous mutation of TFG was identified as the causative gene for autosomal-dominant hereditary motor and sensory neuropathy with proximal dominant involvement. In 2013, a homozygous mutation of TFG was reported in a family with early onset spastic paraplegia, optic atrophy, and neuropathy. Another novel mutation in TFG was discovered in 2014 as a cause of dominant axonal Charcot-Marie-Tooth disease type 2. These findings suggest that mutations of TFG cause ER dysfunction and neurodegeneration in this disease spectrum, which is tightly associated with ER function. Here, we review the clinical phenotypes of these diseases and present recent insights that suggest causal roles of ER dysfunction in TFG-related neurologic disorders. Although the precise pathogenetic mechanisms underlying these TFG mutations remain to be elucidated, experimental manipulations suggest that the dysregulations of ER homeostasis that occur due to mutations in TFG lead to neurodegeneration.Entities:
Keywords: Charcot-Marie-Tooth disease; Endoplasmic reticulum; Neurodegeneration; Spastic paraplegia; Tropomyosin-receptor kinase fused gene (TFG).
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Year: 2016 PMID: 26945032 DOI: 10.1093/jnen/nlw009
Source DB: PubMed Journal: J Neuropathol Exp Neurol ISSN: 0022-3069 Impact factor: 3.685