The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

MAL  -  mal, T-cell differentiation protein

Canis lupus familiaris

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of MAL

  • The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells [1].
 

High impact information on MAL

  • MAL regulates clathrin-mediated endocytosis at the apical surface of Madin-Darby canine kidney cells [2].
  • To maintain its distribution, MAL cycles continuously between the plasma membrane and the Golgi complex [2].
  • Immunoelectron microscopic analysis evidenced colabeling of MAL with apically labeled pIgR in pits and clathrin-coated vesicles [2].
  • The MAL (MAL/VIP17) proteolipid is a nonglycosylated integral membrane protein expressed in a restricted pattern of cell types, including T lymphocytes, myelin-forming cells, and polarized epithelial cells [1].
  • Apical transport of HA was restored to normal levels by expression of MAL with an intact but not with modified carboxyl terminal sequences bearing mutations that impair the functioning of dilysine-based sorting signals, although all the MAL proteins analyzed incorporated efficiently into lipid rafts [3].
 

Chemical compound and disease context of MAL

  • An intact dilysine-like motif in the carboxyl terminus of MAL is required for normal apical transport of the influenza virus hemagglutinin cargo protein in epithelial Madin-Darby canine kidney cells [3].
 

Biological context of MAL

  • The MAL proteolipid, a component of the integral protein sorting machinery, has been demonstrated as being necessary for normal apical transport of the influenza virus hemagglutinin (HA) and the overall apical membrane proteins in Madin-Darby canine kidney (MDCK) cells [3].
  • We found that the expression of the genes such as VIP17/MAL, annexin II, stimulatory GTP binding protein, tubulin, and mitochondrial ATP synthase was induced by AVP treatment for 4h [4].
 

Anatomical context of MAL

 

Associations of MAL with chemical compounds

  • The MAL carboxy terminus ends with the sequence Arg-Trp-Lys-Ser-Ser (RWKSS), which resembles dilysine-based motifs involved in protein sorting [3].
  • Cholesterol sequestration, which blocks apical secretion of Tg, did not alter the levels of MAL in rafts but created a block proximal to Tg entrance into rafts [7].
  • We have examined the secretion of recombinant Tg and gp80/clusterin, a major endogenous secretory protein not detected in Triton X-100 insoluble rafts, for the investigation of the involvement of MAL in the constitutive apical secretory pathway of MDCK cells [7].
  • This means that 47% of the total renal ouabain-binding sites are localized to PT, whereas MAL and DT together contain 51% [8].
 

Regulatory relationships of MAL

  • Apical secretion of gp80/clusterin was also inhibited by elimination of endogenous MAL [7].
 

Analytical, diagnostic and therapeutic context of MAL

  • Analysis by immunofluorescence microscopy of epitope-tagged VIP17/MAL expressed transiently in BHK cells and stably in MDCK cells revealed a perinuclear, vesicular, and plasmalemmal staining [5].

References

  1. The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells. Puertollano, R., Martín-Belmonte, F., Millán, J., de Marco, M.C., Albar, J.P., Kremer, L., Alonso, M.A. J. Cell Biol. (1999) [Pubmed]
  2. MAL regulates clathrin-mediated endocytosis at the apical surface of Madin-Darby canine kidney cells. Martín-Belmonte, F., Martínez-Menárguez, J.A., Aranda, J.F., Ballesta, J., de Marco, M.C., Alonso, M.A. J. Cell Biol. (2003) [Pubmed]
  3. An intact dilysine-like motif in the carboxyl terminus of MAL is required for normal apical transport of the influenza virus hemagglutinin cargo protein in epithelial Madin-Darby canine kidney cells. Puertollano, R., Martínez-Menárguez, J.A., Batista, A., Ballesta, J., Alonso, M.A. Mol. Biol. Cell (2001) [Pubmed]
  4. Identification of vasopressin-induced genes in AQP2-transfected MDCK cells by suppression subtractive hybridization. Kang, D.Y., Park, J.I., Cho, W.S., Jeong, M.H., Cho, G.W., Park, H.T., Bae, H.R. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  5. VIP17/MAL, a proteolipid in apical transport vesicles. Zacchetti, D., Peränen, J., Murata, M., Fiedler, K., Simons, K. FEBS Lett. (1995) [Pubmed]
  6. Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL. Tall, R.D., Alonso, M.A., Roth, M.G. Traffic (2003) [Pubmed]
  7. MAL mediates apical transport of secretory proteins in polarized epithelial Madin-Darby canine kidney cells. Martín-Belmonte, F., Arvan, P., Alonso, M.A. J. Biol. Chem. (2001) [Pubmed]
  8. Distribution of ouabain-binding sites along the dog nephron. Sejersted, O.M., Nicolaysen, A., Monclair, T., Nicolaysen, G. Acta Physiol. Scand. (1985) [Pubmed]
 
WikiGenes - Universities