B6.D2-Scn8a^med-jo/J

Stock number: 003799
Product name: jolting
Research areas: Cell Biology Research, Neurobiology Research

Description

Jolting mice carry a spontaneous, autosomal recessive mutation characterized by cerebellar ataxia and generalized tremor and exhibit progressive weakness due to a functional denervation of skeletal muscle attributed to abnormalities in the cerebellum.

Detailed description

Jolting mice carry a spontaneous, autosomal recessive mutation characterized by cerebellar ataxia and generalized tremor and exhibit progressive weakness due to a functional denervation of skeletal muscle. The mutation results in substitution of Thr for an evolutionarily conserved Ala residue in the cytoplasmic S4-S5 linker of domain III. Abnormalities in the cerebellum are responsible for the gait problems of the jolting mouse, and preliminary morphological and neurophysiological examination of the mouse with motor end-plate disease has shown that it also has cerebellar abnormalities. Axonal spheroids may be seen on cerebellar Purkinje cell axons, and the character of extra-cellular recordings obtained from the Purkinje cells is abnormal.

Development

The Scn8a^med-jo mutation arose spontaneously in DBA/2WyDi. John Harris maintained this allele in Newcastle, UK from the early 1970s then passed it off to M Meisler. In March, 2000 The Jackson Laboratory received from M. Meisler heterozygous males labeled N5 which have been bred to C57BL/6J and are now maintained via backcross intercross.

Allele

Symbol: Scn8a^med-jo
Name: jolting
MGI accession ID: MGI:1856080
Generation method: Spontaneous
Marker symbol: Scn8a
Marker name: sodium channel, voltage-gated, type VIII, alpha
Chromosome: 15
Strain of origin: DBA/2WyDi
Molecular note: A transition point mutation that altered coding nucleotide 3949 from G-to-A, which replaces the alanine at residue 1317 with threonine (p.A1317T). The mutation is located in a region of the ion channel that is predicted to encode the cytoplasmic linker between integral membrane segments S4 and S5 in domain III.