High impact information on Llgl1

• These phosphorylation sites are important for embryonic fibroblasts to polarize correctly in response to wounding and may regulate the ability of Mlgl to direct protein trafficking [1].
• Here we identify direct physiological interactions between mammalian aPKC, murine Par-6C (mPar-6C) and Mlgl, the mammalian orthologue of the Drosophila melanogaster tumour suppressor Lethal (2) giant larvae [1].
• Membrane-bound Mlgl from MDCK cell lysates was coimmunoprecipitated with syntaxin 4, a component of the exocytic machinery at the basolateral membrane, but not with other plasma membrane soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) proteins that are either absent from or not restricted to the basolateral membrane domain [2].
• Herein, we characterize a mammalian homolog of l(2)gl, called Mlgl, in the epithelial cell line Madin-Darby canine kidney (MDCK) [2].
• These data suggest that Mlgl contributes to apico-basolateral polarity by regulating basolateral exocytosis [2].

Biological context of Llgl1

• We have isolated and characterized the human homologue of the murine Llglh gene, which was originally isolated as a homologue of a Drosophila tumor suppressor gene 1(2)gl (lethal(2) giant larvae) [3].
• In our FISH analysis of metaphase chromosomes of four SMS patients, a probe representing LLGL failed in each case to hybridize to one of the two chromosome 17 homologues, indicating that this gene may play a role in the pathogenesis of SMS [3].
• Phosphorylation within a highly conserved region of Mlgl is required to restrict the protein to the lateral domain, because a recombinant phospho-mutant is distributed in a nonpolar manner [2].
• Consistent with a role in cell polarity, Mlgl redistributes from a cytoplasmic localization to the lateral membrane after contact-naive MDCK cells make cell-cell contacts and establish a polarized phenotype [2].
• Fliih, the murine homologue of the Drosophila melanogaster flightless I gene: nucleotide sequence, chromosomal mapping and overlap with Llglh [4].

Associations of Llgl1 with chemical compounds

• Interestingly, mutant forms of Mgl-1 at the conserved glycine at position 450 and aspartic acid at position 453 in the most conserved WD-40 repeat motif were not able to complement, indicating that these amino acids are critical for regulating salt tolerance and temperature sensitivity in yeast [5].

Other interactions of Llgl1

• In the mouse, Llglh is thought to play an important role during brain development as a regulatory target of Hoxc8 [3].
• Fliih lies adjacent to Llglh, the mouse homologue of the D. melanogaster tumor suppressor gene lethal(2) giant larvae [4].

References