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

• Immunohistochemical staining and in situ hybridization show that MALS occur differentially in discrete populations of neurons throughout the brain [4].
• Using site-directed mutagenesis, we have identified the conserved residues among these proteins crucial for mLin-7 binding [6].
• Molecular cloning and characterization of Pals, proteins associated with mLin-7 [6].

References