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Gene Review

Lin7a  -  lin-7 homolog A (C. elegans)

Mus musculus

Synonyms: AI848705, LIN-7A, Lin-7A, MALS-1, Mals1, ...
 
 
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High impact information on Lin7a

  • Instead, beta-catenin modulates vesicle localization via its PDZ binding domain to recruit PDZ proteins such as Veli to cadherin at synapses [1].
  • In this study, we purified the MALS protein complex from brain and found liprin-alpha as a major component [2].
  • The MALS/Veli-CASK-Mint-1 complex of PDZ proteins occurs on both sides of the synapse and has the potential to link transsynaptic adhesion molecules to the cytoskeleton [2].
  • Fittingly, mutant mice lacking all three MALS isoforms died perinatally with difficulty breathing and impaired excitatory synaptic transmission [2].
  • In this report, we further define the binding of the L27C domain of mLin-2/CASK to the L27 domain of mLin-7 and identify the binding partner for L27N of mLin-2/CASK [3].
 

Biological context of Lin7a

  • Targeted disruption of MALS-1 and MALS-2 does not yield a detectable phenotype, and hippocampal synaptic function and plasticity are intact in the MALS-1/2 double knockouts [4].
 

Anatomical context of Lin7a

  • Marked prolongation of islet xenograft survival in the spleen can be achieved with in vitro culture (24 C) and a single injection of either rabbit antiserum to mouse lymphocytes (MALS) alone or MALS and rabbit antiserum to rat lymphocytes (RALS) into the recipients [5].
 

Associations of Lin7a with chemical compounds

  • Pals proteins represent a new subfamily of membrane-associated guanylate kinases that allow for multiple targeting complexes containing mLin-7 [6].
 

Regulatory relationships of Lin7a

  • Interestingly, MALS-3 protein is dramatically induced in the MALS-1/2 double knockouts, implying that dynamic changes in protein expression may play an important regulatory role for this family of synaptic PDZ proteins [4].
 

Other interactions of Lin7a

  • In mouse brain, we have identified a heterotrimeric complex that contains mLin-2, mLin-7, and X11alpha and that is likely important for the localization of proteins in polarized cells [7].
  • Furthermore, we can detect direct interactions between mLin-2 and mammalian Lin-7 (mLin-7) [7].
  • Neurotransmitter release regulated by a MALS-liprin-alpha presynaptic complex [2].
 

Analytical, diagnostic and therapeutic context of Lin7a

References

  1. Role of beta-catenin in synaptic vesicle localization and presynaptic assembly. Bamji, S.X., Shimazu, K., Kimes, N., Huelsken, J., Birchmeier, W., Lu, B., Reichardt, L.F. Neuron (2003) [Pubmed]
  2. Neurotransmitter release regulated by a MALS-liprin-alpha presynaptic complex. Olsen, O., Moore, K.A., Fukata, M., Kazuta, T., Trinidad, J.C., Kauer, F.W., Streuli, M., Misawa, H., Burlingame, A.L., Nicoll, R.A., Bredt, D.S. J. Cell Biol. (2005) [Pubmed]
  3. A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia. Lee, S., Fan, S., Makarova, O., Straight, S., Margolis, B. Mol. Cell. Biol. (2002) [Pubmed]
  4. Contrasting localizations of MALS/LIN-7 PDZ proteins in brain and molecular compensation in knockout mice. Misawa, H., Kawasaki, Y., Mellor, J., Sweeney, N., Jo, K., Nicoll, R.A., Bredt, D.S. J. Biol. Chem. (2001) [Pubmed]
  5. Prolongation of intrasplenic islet xenograft survival. Janney, C.G., Lacy, P.E., Finke, E.H., Davie, J.M. Am. J. Pathol. (1982) [Pubmed]
  6. Molecular cloning and characterization of Pals, proteins associated with mLin-7. Kamberov, E., Makarova, O., Roh, M., Liu, A., Karnak, D., Straight, S., Margolis, B. J. Biol. Chem. (2000) [Pubmed]
  7. Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting. Borg, J.P., Straight, S.W., Kaech, S.M., de Taddéo-Borg, M., Kroon, D.E., Karnak, D., Turner, R.S., Kim, S.K., Margolis, B. J. Biol. Chem. (1998) [Pubmed]
 
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