MAL (gene)

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Mal, T-cell differentiation protein
Identifiers
Symbol(s) MAL;
External IDs OMIM: 188860 MGI892970 HomoloGene7827
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 4118 17153
Ensembl ENSG00000172005 ENSMUSG00000027375
Uniprot P21145 Q545Q7
Refseq NM_002371 (mRNA)
NP_002362 (protein)
NM_010762 (mRNA)
NP_034892 (protein)
Location Chr 2: 95.06 - 95.08 Mb Chr 2: 127.32 - 127.35 Mb
Pubmed search [1] [2]

Mal, T-cell differentiation protein, also known as MAL, is a human gene.[1]

The protein encoded by this gene is a highly hydrophobic integral membrane protein belonging to the MAL family of proteolipids. The protein has been localized to the endoplasmic reticulum of T-cells and is a candidate linker protein in T-cell signal transduction. In addition, this proteolipid is localized in compact myelin of cells in the nervous system and has been implicated in myelin biogenesis and/or function. The protein plays a role in the formation, stabilization and maintenance of glycosphingolipid-enriched membrane microdomains. Alternative splicing produces four transcript variants which vary from each other by the presence or absence of alternatively spliced exons 2 and 3.[1]

[edit] References

[edit] Further reading

  • Frank M (2000). "MAL, a proteolipid in glycosphingolipid enriched domains: functional implications in myelin and beyond.". Prog. Neurobiol. 60 (6): 531-44. PMID 10739088. 
  • Alonso MA, Barton DE, Francke U (1988). "Assignment of the T-cell differentiation gene MAL to human chromosome 2, region cen----q13.". Immunogenetics 27 (2): 91-5. PMID 3257199. 
  • Alonso MA, Weissman SM (1987). "cDNA cloning and sequence of MAL, a hydrophobic protein associated with human T-cell differentiation.". Proc. Natl. Acad. Sci. U.S.A. 84 (7): 1997-2001. PMID 3494249. 
  • Rancaño C, Rubio T, Alonso MA (1994). "Alternative splicing of human T-cell-specific MAL mRNA and its correlation with the exon/intron organization of the gene.". Genomics 21 (2): 447-50. doi:10.1006/geno.1994.1294. PMID 8088843. 
  • Rancaño C, Rubio T, Correas I, Alonso MA (1994). "Genomic structure and subcellular localization of MAL, a human T-cell-specific proteolipid protein.". J. Biol. Chem. 269 (11): 8159-64. PMID 8132541. 
  • Millán J, Puertollano R, Fan L, et al. (1997). "The MAL proteolipid is a component of the detergent-insoluble membrane subdomains of human T-lymphocytes.". Biochem. J. 321 ( Pt 1): 247-52. PMID 9003426. 
  • Millán J, Puertollano R, Fan L, Alonso MA (1997). "Caveolin and MAL, two protein components of internal detergent-insoluble membranes, are in distinct lipid microenvironments in MDCK cells.". Biochem. Biophys. Res. Commun. 233 (3): 707-12. doi:10.1006/bbrc.1997.6530. PMID 9168919. 
  • Martín-Belmonte F, Kremer L, Albar JP, et al. (1998). "Expression of the MAL gene in the thyroid: the MAL proteolipid, a component of glycolipid-enriched membranes, is apically distributed in thyroid follicles.". Endocrinology 139 (4): 2077-84. PMID 9528996. 
  • Köhler C, Håkansson A, Svanborg C, et al. (1999). "Protease activation in apoptosis induced by MAL.". Exp. Cell Res. 249 (2): 260-8. doi:10.1006/excr.1999.4472. PMID 10366425. 
  • Frank M, Schaeren-Wiemers N, Schneider R, Schwab ME (1999). "Developmental expression pattern of the myelin proteolipid MAL indicates different functions of MAL for immature Schwann cells and in a late step of CNS myelinogenesis.". J. Neurochem. 73 (2): 587-97. PMID 10428054. 
  • Puertollano R, Alonso MA (1999). "MAL, an integral element of the apical sorting machinery, is an itinerant protein that cycles between the trans-Golgi network and the plasma membrane.". Mol. Biol. Cell 10 (10): 3435-47. PMID 10512878. 
  • Erne B, Sansano S, Frank M, Schaeren-Wiemers N (2002). "Rafts in adult peripheral nerve myelin contain major structural myelin proteins and myelin and lymphocyte protein (MAL) and CD59 as specific markers.". J. Neurochem. 82 (3): 550-62. PMID 12153479. 
  • Copie-Bergman C, Plonquet A, Alonso MA, et al. (2003). "MAL expression in lymphoid cells: further evidence for MAL as a distinct molecular marker of primary mediastinal large B-cell lymphomas.". Mod. Pathol. 15 (11): 1172-80. doi:10.1097/01.MP.0000032534.81894.B3. PMID 12429796. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Kazemi-Noureini S, Colonna-Romano S, Ziaee AA, et al. (2004). "Differential gene expression between squamous cell carcinoma of esophageus and its normal epithelium; altered pattern of mal, akr1c2, and rab11a expression.". World J. Gastroenterol. 10 (12): 1716-21. PMID 15188492. 
  • Llorente A, de Marco MC, Alonso MA (2005). "Caveolin-1 and MAL are located on prostasomes secreted by the prostate cancer PC-3 cell line.". J. Cell. Sci. 117 (Pt 22): 5343-51. doi:10.1242/jcs.01420. PMID 15466889. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Dukhovny A, Goldstein Magal L, Hirschberg K (2006). "The MAL proteolipid restricts detergent-mediated membrane pore expansion and percolation.". Mol. Membr. Biol. 23 (3): 245-57. doi:10.1080/09687860600601445. PMID 16785208. 
  • Mimori K, Nishida K, Nakamura Y, et al. (2007). "Loss of MAL expression in precancerous lesions of the esophagus.". Ann. Surg. Oncol. 14 (5): 1670-7. doi:10.1245/s10434-006-9064-2. PMID 17151798.