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Gene Review

LRRC7  -  leucine rich repeat containing 7

Homo sapiens

Synonyms: Densin, Densin-180, KIAA1365, LAP1, Leucine-rich repeat-containing protein 7, ...
 
 
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Disease relevance of LRRC7

  • Latency-associated promoter 1 (LAP1) of herpes simplex virus type 1 is required to generate a series of latency-associated transcripts (LATs) in sensory neurons of latently infected animals [1].
 

High impact information on LRRC7

  • The sequence of densin-180 contains 17 leucine-rich repeats, a sialomucin domain, an apparent transmembrane domain, and a PDZ domain [2].
  • Immunocytochemical localization of densin-180 in dissociated hippocampal neuronal cultures shows that the protein is highly concentrated at synapses along dendrites [2].
  • The message encoding densin-180 is brain specific and is more abundant in forebrain than in cerebellum [2].
  • We propose that densin-180 participates in specific adhesion between presynaptic and postsynaptic membranes at glutamatergic synapses [2].
  • We present a detailed comparative analysis of the PDZ domains of the human LAP proteins Erbin, Densin-180, and Scribble and the MAGUK ZO-1 [3].
 

Biological context of LRRC7

  • Densin-180, a protein purified from the postsynaptic density fraction of the rat forebrain, is the founding member of a newly described family of proteins termed the LAP (leucine-rich repeats and PSD-95/Dlg-A/ZO-1 (PDZ) domains) family that plays essential roles in establishment of cell polarity [4].
  • Although Densin-180 was reported to be a transmembrane protein, Densin-180 was not accessible to surface biotinylation in dissociated hippocampal neurons; hence Densin-180 may be a cytosolic protein [4].
  • We have cloned a novel splice variant of densin-180 from a fetal brain cDNA library and termed it LRRC7 [5].
  • In contrast, phosphorylation of densin-180 by CaMKII at serine-1397 only slightly decreases its affinity for CaMKII [6].
  • We demonstrate by yeast two-hybrid and biochemical assays that the intracellular portion of densin-180, the alpha-subunit of CaMKII (CaMKIIalpha), and alpha-actinin interact with each other at distinct binding sites and can form a ternary complex stabilized by multiple interactions [6].
 

Anatomical context of LRRC7

  • The specific interaction of densin-180 with holoenzymes of CaMKII containing only alpha-subunit and the increased affinity of CaMKII for densin-180 after autophosphorylation suggest that densin-180 may be involved in localization of activated CaMKII synthesized in dendrites [6].
  • The N-terminal leucine-rich repeat region, which is not involved in binding shank, targets Densin-180 to the plasma membrane in transfected cells and to the basolateral membrane of epithelial cells [7].
 

Associations of LRRC7 with chemical compounds

  • The soybean (Glycine max (L.) Merrill) seed leucine aminopeptidase locus (Lap1) was found to be linked to the Kunitz trypsin inhibitor locus (Ti) with a recombination frequency of 15.3 percent +/- 0.9 percent [8].
 

Physical interactions of LRRC7

  • Densin-180 PDZ domain binds the COOH terminus of delta-catenin/NPRAP containing the PDZ domain-binding sequence [4].
  • Here we report the identification of the alpha-subunit of Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) and alpha-actinin-4 as potential binding partners for the densin-180 intracellular segment [6].
 

Other interactions of LRRC7

  • Coexpression of shank3 abrogates branch formation and targets Densin-180 into postsynaptic clusters instead [7].
  • Leucine-rich repeat and PDZ [postsynaptic density-95 (PSD-95)/Discs large/zona occludens-1] domain proteins such as scribble and Densin-180 have been implicated in the establishment of cell-cell contacts [7].
  • In mammals, three LAP proteins have been described, Densin-180, Erbin, and hScribble [9].
 

Analytical, diagnostic and therapeutic context of LRRC7

  • Sequence analysis and DNA binding studies have suggested the existence of several cis-acting elements within LAP1 that are potentially important for promoter function, although their role in LAT gene expression during latency is largely unexplored [1].
  • A reduction in LAT synthesis measured by in situ hybridization and reverse transcription-PCR (RT-PCR) of rat brain tissue latently infected with a LAP1 TATA substitution virus demonstrated that this sequence was required for full LAP1 activity in vivo [1].

References

  1. cis-acting elements involved in transcriptional regulation of the herpes simplex virus type 1 latency-associated promoter 1 (LAP1) in vitro and in vivo. Soares, K., Hwang, D.Y., Ramakrishnan, R., Schmidt, M.C., Fink, D.J., Glorioso, J.C. J. Virol. (1996) [Pubmed]
  2. Characterization of densin-180, a new brain-specific synaptic protein of the O-sialoglycoprotein family. Apperson, M.L., Moon, I.S., Kennedy, M.B. J. Neurosci. (1996) [Pubmed]
  3. Convergent and divergent ligand specificity among PDZ domains of the LAP and zonula occludens (ZO) families. Zhang, Y., Yeh, S., Appleton, B.A., Held, H.A., Kausalya, P.J., Phua, D.C., Wong, W.L., Lasky, L.A., Wiesmann, C., Hunziker, W., Sidhu, S.S. J. Biol. Chem. (2006) [Pubmed]
  4. Densin-180 interacts with delta-catenin/neural plakophilin-related armadillo repeat protein at synapses. Izawa, I., Nishizawa, M., Ohtakara, K., Inagaki, M. J. Biol. Chem. (2002) [Pubmed]
  5. Cloning and characterization of a novel splice variant of the brain-specific protein densin-180. Wang, L., Xu, J., Wu, Q., Dai, J., Ye, X., Zeng, L., Ji, C., Gu, S., Zhao, R.C., Xie, Y., Mao, Y. Int. J. Mol. Med. (2003) [Pubmed]
  6. Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin. Walikonis, R.S., Oguni, A., Khorosheva, E.M., Jeng, C.J., Asuncion, F.J., Kennedy, M.B. J. Neurosci. (2001) [Pubmed]
  7. Postsynaptic shank antagonizes dendrite branching induced by the leucine-rich repeat protein Densin-180. Quitsch, A., Berhörster, K., Liew, C.W., Richter, D., Kreienkamp, H.J. J. Neurosci. (2005) [Pubmed]
  8. Genetic linkage of a leucine aminopeptidase locus with the Kunitz trypsin inhibitor locus in soybeans. Kiang, Y.T., Chiang, Y.C. J. Hered. (1986) [Pubmed]
  9. Lano, a novel LAP protein directly connected to MAGUK proteins in epithelial cells. Saito, H., Santoni, M.J., Arsanto, J.P., Jaulin-Bastard, F., Le Bivic, A., Marchetto, S., Audebert, S., Isnardon, D., Adélaïde, J., Birnbaum, D., Borg, J.P. J. Biol. Chem. (2001) [Pubmed]
 
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