Disease relevance of SMU1

• At re-test there was a decrease from 48% to 39% of body weight distribution (%BWD) on the paretic leg in rising and in sitting down in the patients in the auditory feedback group (p < 0.001) [1].

High impact information on SMU1

• The SMU-1 amino acid sequence is more than 60% identical to a predicted human protein of unknown function [2].
• Temperature-sensitive CHO-K1 mutant cell line tsTM18 exhibits chromosomal instability and cell-cycle arrest at S and G2 phases with decreased DNA synthesis at the nonpermissive temperature, 39 degrees C. We previously identified an amino acid substitution in Smu1 that underlies the temperature-sensitive phenotypes of tsTM18 cells [3].
• In the present study, we confirmed that Smu1 is associated with the temperature-sensitive defect of tsTM18 by RNA interference [3].
• Analysis of chromosome content of temperature-resistant transformants and introduction of a bacterial artificial chromosome containing part of human chromosome 9 led to isolation of the human SMU1 gene [4].
• A temperature-sensitive mutation in the WD repeat-containing protein Smu1 is related to maintenance of chromosome integrity [4].

Biological context of SMU1

• Comparison of sequences of the Smu1 gene from wild-type and mutant cells revealed that the mutant phenotype is caused by a G-to-A transition that yields a gly-to-arg substitution at position 489 in hamster Smu1 [4].
• Even so, Smu1, though not absolutely required for mating, is necessary for wild-type mating and pathogenicity [5].

Anatomical context of SMU1

• Also, the FHL and PLT, along with the soleus (SOL; also recorded in this study), contributed to an extensor muscle torque (described in paper IV of this series) and the generation of mechanical power at the ankle joint during stance of FWD and BWD walking [6].

Associations of SMU1 with chemical compounds

• The substituted glycine is located in the WD-repeat domain of Smu1 [4].
• Their recruitment contributed to the flexor muscle torque at the MTP joint during most of FWD and BWD stance and was responsible for the absorption of mechanical power at the MTP joint for FWD stance and generation of mechanical power at the MTP joint during BWD stance [6].
• This substance, BWD II 22-3, which was composed of Asp(1), Thr(1), Ser(1), Gly(1), Gly(4), Ala(1), Val(1), Leu(1), Orn(2), Lys(1), Arg(1), Cys(1) and glucose was demonstrated to be homogeneous by gel filtration and paper electrophoretic analyses [7].

Other interactions of SMU1

• Mutation analysis in three other candidate genes (beta-tropomyosin, NDUFB6 and SMU1) did not identify any mutations [8].

Analytical, diagnostic and therapeutic context of SMU1

• In cryosections of rat cerebellum and kidney, BWD is shown by immunohistochemistry to be localized in the nucleus and cytoplasm of cerebellar Purkinje and granule neurons, and in predominantly the cytoplasm of cells surrounding kidney ducts [9].
• An active component, BWD II 22-3, might prove effective in the hyposensitization therapy of buckwheat-sensitive patients [7].
• In the control group the decrease was from 44 to 39% BWD on the paretic leg (p < 0.05) in rising and from 44 to 42% BWD (n.s.) in sitting down [1].

References