LRRC32 (Leucine-Rich Repeat Containing 32) is a Protein Coding gene. This gene encodes a type I membrane protein which contains 20 leucine-rich repeats. LRRC32, also known as Glycoprotein A Repetitions Predominant (GARP), has been postulated as a novel surface marker of activated T(regs). LRRC32 is a T(reg)-specific receptor that binds latent TGF-beta and dominantly controls FOXP3 and the regulatory phenotype via a positive feedback loop. It belongs to the LRRC32/LRRC33 family and is broadly expressed in the placenta, lung, and other tissues. Alterations in the chromosomal region 11q13-11q14 are involved in several pathologies. An important paralog of this gene is NRROS.
Leucine-Rich Repeat-Containing Protein 3B (LRRC3B) belongs to the LRRC3 family. LRRC3B is single-pass membrane protein and contains three leucine-rich repeats, one LRRCT domain, and one LRRNT domain. LRR-containing proteins, of which there are greater than 2,000, participate in many important processes, including plant and animal immunity, hormone-receptor interactions, cell adhesion, signal transduction, regulation of gene expression, and apoptosis. A number of microarray expression profiling studies on human cancers have shown that LRRC3B is down-regulated in gastric, breast, colon, testis, prostate and brain cancers, suggesting LRRC3B involvement in carcinogenesis
Leucine-Rich Repeat Transmembrane Neuronal Protein 2 (LRRTM2) is a single-pass type I membrane protein that belongs to the LRRTM family. It contains ten LRR (leucine-rich) repeats, one LRRCT domain, and one LRRNT domain. LRRTM2 is expressed in neuronal tissues, and it interacts with DLG4 and NRXN1. LRRTM2 has been suggested to be involved in the development and maintenance of excitatory synapses in the vertebrate nervous system. LRRTM2 also regulates the surface expression of AMPA receptors. LRRTM2 acts as a ligand for the presynaptic receptors NRXN1-A and NRXN1-B.
Leucine-rich repeat neuronal protein 3, also known as neuronal leucine-rich repeat protein 3 (NLRR-3), is a member of leucine-rich (LRR) family whose members have significant functions in neural development. Leucine-rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. All proteins containing these repeats are thought to be involved in protein-protein interactions. The crystal structure of ribonuclease inhibitor protein has revealed that leucine-rich repeats correspond to β-α structural units. These units are arranged so that they form a parallel β-sheet with one surface exposed to solvent, so that the protein acquires an unusual, non-globular shape. These two features may be responsible for the protein-binding functions of proteins containing leucine-rich repeats. LRRN3 plays an important role in cerebellum postnatal development. In a unilateral cortical injury cerebral cortex, NLRR-3 mRNA increased in layers 2-3 which suggests that NLRR-3 may be an important component of the pathophysiological response to brain injury.
Leucine-rich repeat transmembrane neuronal protein 4, also known as LRRTM4, is a single-pass type I membrane protein which belongs to theLRRTM family. LRRTM4 is expressed in the limb mesenchyme, neural tube, caudal mesoderm and in three distinct regions of the head. LRRTM4 may play a role in the development and maintenance of the vertebrate nervous system. Leucine-rich repeat containing proteins are involved in protein-protein interactions and they regulate numerous cellular events during nervous system development and disease. Human and mouse LRRTMs are highly conserved, and orthologous genes exist in other vertebrates but not in invertebrates. LRRTM mRNAs are predominantly expressed in the nervous system and that each LRRTM possesses a specific, partially nonoverlapping expression pattern. The structure and expression profile of LRRTM mRNAs suggest that they may have a role in the development and maintenance of the vertebrate nervous system. All LRRTMs, except LRRTM4, are located in the introns of different alpha-catenin genes, suggesting coevolution of these two gene families.
The limbic system-associated membrane protein (LAMP) is a cell surface glycoprotein expressed by cortical and subcortical regions of the mammalian CNS that comprise or receive direct projections from limbic system structures. The 64-68-kDa glycoprotein limbic system-associated membrane protein (LsAMP) is expressed on the surface of somata and proximal dendrites of neurons. These areas perform cognitive and autonomic functions; also learning and memory. The functional analysis indicates that LsAMP acts as a selective adhesion molecule; serving as a guidance cue for specific patterns of connectivity; which underlies the normal development of the limbic system. In animal studies there have been found that rats with increased level of anxiety had 1.6-fold higher expression of LsAMP gene in the periaqueductal gray compared to rats with low level of anxiety; indicating a possible role of LsAMP in the regulation of anxiety.
Limbic system-associated membrane protein is also known as LSAMP; IgLON family member 3. In humans; it is encoded by the LSAMP gene. It belongs to the immunoglobulin superfamily and contains 3 Ig-like C2-type domains. Limbic system-associated membrane protein mediates selective neuronal growth and axon targeting. It contributes to the guidance of developing axons and remodeling of mature circuits in the limbic system. It is also essential for normal growth of the hyppocampal mossy fiber projection
U6 snRNA-Associated Sm-Like Protein LSm1 (LSM1) belongs to the snRNP Sm proteins family. The Sm-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which plays an important role in pre-mRNA splicing. LSM1 binds specifically to the 3-terminal U-tract of U6snRNA. LSM1 can interact with SLBP when histone mRNA is being rapidly degraded during the S phase. In addition, LSM1 is associated with cellular transformation and the progression of several malignancies including mesothelioma, lung cancer and breast cancer.
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