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Bloc1s3  -  biogenesis of lysosomal organelles complex...

Mus musculus

Synonyms: BC043666, BLOC-1 subunit 3, BLOS3, Biogenesis of lysosome-related organelles complex 1 subunit 3, Blos3, ...
 
 
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High impact information on Bloc1s3

  • Interestingly, eye pigment formation is reported to be normal in rp, but we found visual defects (nystagmus, iris transilluminancy, foveal hypoplasia, reduced visual acuity, and evidence of optic pathway misrouting) in affected individuals [1].
  • We show that the wild-type rp gene encodes a novel, widely expressed 195-amino acid protein that shares 87% amino acid identity with its human orthologue and localizes to punctate cytoplasmic structures [2].
  • A possible relationship between this mode of translational control and the selective suppression of rp mRNA translation by glucocorticoids is discussed [3].
  • In the present experiments we examined whether dexamethasone treatment causes any alteration in the accumulation or utilization of mRNAs that encode ribosomal proteins (rp mRNAs) [3].
  • In untreated or fully recovered cells, the distribution of rp mRNAs between polyribosomes and free ribonucleoprotein is distinctly bimodal, suggesting that rp mRNAs are subject to a particular form of translational control in which they are either translationally inactive or fully loaded with ribosomes [3].
 

Biological context of Bloc1s3

 

Anatomical context of Bloc1s3

  • We found that about 85% of pulse-labeled rp mRNA was associated with polysomes in exponentially growing cells [4].
  • Furthermore, the level of S29 rp mRNA was downregulated in rapidly proliferating HT29 cells, as compared to the contact inhibited cells [6].
 

Other interactions of Bloc1s3

  • Beige, bg, and reduced pigmentation, rp, are recessive mutations affecting lysosomal function [7].
 

Analytical, diagnostic and therapeutic context of Bloc1s3

  • Northern blot analysis showed that the level of S29 rp mRNA was higher in undifferentiated HT29 human colon carcinoma cells than in a morphologically differentiated subclone under the same growth condition [6].

References

  1. A germline mutation in BLOC1S3/reduced pigmentation causes a novel variant of Hermansky-Pudlak syndrome (HPS8). Morgan, N.V., Pasha, S., Johnson, C.A., Ainsworth, J.R., Eady, R.A., Dawood, B., McKeown, C., Trembath, R.C., Wilde, J., Watson, S.P., Maher, E.R. Am. J. Hum. Genet. (2006) [Pubmed]
  2. Reduced pigmentation (rp), a mouse model of Hermansky-Pudlak syndrome, encodes a novel component of the BLOC-1 complex. Gwynn, B., Martina, J.A., Bonifacino, J.S., Sviderskaya, E.V., Lamoreux, M.L., Bennett, D.C., Moriyama, K., Huizing, M., Helip-Wooley, A., Gahl, W.A., Webb, L.S., Lambert, A.J., Peters, L.L. Blood (2004) [Pubmed]
  3. Glucocorticoids selectively inhibit translation of ribosomal protein mRNAs in P1798 lymphosarcoma cells. Meyuhas, O., Thompson, E.A., Perry, R.P. Mol. Cell. Biol. (1987) [Pubmed]
  4. Regulation of ribosomal protein mRNA content and translation in growth-stimulated mouse fibroblasts. Geyer, P.K., Meyuhas, O., Perry, R.P., Johnson, L.F. Mol. Cell. Biol. (1982) [Pubmed]
  5. Combined cochleo-saccular and neuroepithelial abnormalities in the Varitint-waddler-J (VaJ) mouse. Cable, J., Steel, K.P. Hear. Res. (1998) [Pubmed]
  6. The S29 ribosomal protein increases tumor suppressor activity of K rev-1 gene on v-K ras-transformed NIH3T3 cells. Kondoh, N., Noda, M., Fisher, R.J., Schweinfest, C.W., Papas, T.S., Kondoh, A., Samuel, K.P., Oikawa, T. Biochim. Biophys. Acta (1996) [Pubmed]
  7. Lysosomal mutations inhibit lipofuscinosis of the spleen in C57BL mice. Ahmed, F., Shire, J.G. J. Hered. (1985) [Pubmed]
 
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