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Stard3  -  START domain containing 3

Mus musculus

Synonyms: Es64, Mln64, Protein ES 64, Protein MLN 64, START domain-containing protein 3, ...
 
 
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Disease relevance of Stard3

  • In this case, the high levels of MLN64 observed in some breast carcinomas could contribute to the progression of these tumors through increased intratumoral steroidogenesis [1].
 

High impact information on Stard3

  • The x-ray structure of the mouse cholesterol-regulated START protein 4 (StarD4) has been determined at 2.2-A resolution, revealing a compact alpha/beta structure related to the START domain present in the cytoplasmic C-terminal portion of human MLN64 [2].
  • Embryonic fibroblast cells transfected with the cholesterol side-chain cleavage system and primary cultures of granulosa cells from Mln64 mutant mice showed defects in sterol trafficking as reflected in reduced conversion of endogenous cholesterol to steroid hormones [3].
  • As MLN64, MENTHO is ubiquitously expressed and is located in the membrane of late endosomes, its amino and carboxyl-terminal extremities projecting toward the cytoplasm [4].
  • MLN64 and MENTHO share 70% identity and 83% similarity in an original protein domain encompassing 171 amino acids that we designated as the MENTAL (MLN64 N-terminal) domain [4].
  • Furthermore, we found MLN64 to be expressed in the adult brain as well, apparently at higher levels than StAR [5].
 

Biological context of Stard3

  • The MLN64 gene, which is localized in q12-q21 of the human chromosome 17, encodes a novel protein containing 2 distinct domains [1].
 

Anatomical context of Stard3

  • In the present study, the presence of StAR and for the first time, its homolog, the putative cholesterol transport protein metastatic lymph node 64 (MLN64), were defined in the neonatal mouse brain using immunocytochemical techniques [5].
 

Associations of Stard3 with chemical compounds

  • These observations suggest that the Mln64 START domain is largely dispensable for sterol metabolism in mice [3].
  • At the N-terminal, MLN64 exhibits a potential trans-membrane region, while at the C-terminal, it shares homology with the F26F4.4 protein of Coenorhabditis elegans and the steroidogenic acute regulatory (StAR) protein, a mitochondrial protein which is involved in steroid-hormone synthesis [1].

References

  1. MLN64 exhibits homology with the steroidogenic acute regulatory protein (STAR) and is over-expressed in human breast carcinomas. Moog-Lutz, C., Tomasetto, C., Régnier, C.H., Wendling, C., Lutz, Y., Muller, D., Chenard, M.P., Basset, P., Rio, M.C. Int. J. Cancer (1997) [Pubmed]
  2. Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain. Romanowski, M.J., Soccio, R.E., Breslow, J.L., Burley, S.K. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  3. Targeted mutation of the MLN64 START domain causes only modest alterations in cellular sterol metabolism. Kishida, T., Kostetskii, I., Zhang, Z., Martinez, F., Liu, P., Walkley, S.U., Dwyer, N.K., Blanchette-Mackie, E.J., Radice, G.L., Strauss, J.F. J. Biol. Chem. (2004) [Pubmed]
  4. MENTHO, a MLN64 homologue devoid of the START domain. Alpy, F., Wendling, C., Rio, M.C., Tomasetto, C. J. Biol. Chem. (2002) [Pubmed]
  5. The steroidogenic acute regulatory protein is expressed in steroidogenic cells of the day-old brain. King, S.R., Ginsberg, S.D., Ishii, T., Smith, R.G., Parker, K.L., Lamb, D.J. Endocrinology (2004) [Pubmed]
 
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