Disease relevance of LNX1

• Thus, LNX might act as a diagnostic marker and a potential therapeutic target for glioma [1].
• OBJECTIVE: The purpose of this study is to assess the survival experience following systematic lymphadenectomy (LNX) in conjunction with primary but optimal cytoreductive surgery in advanced epithelial ovarian cancer (OC) patients when followed by intensive chemotherapy [2].
• Group D (n = 16), TAH, BSO, OMTX, LNX with maximal efforts made to reduce the size of the residual tumor to less than 2 cm at the primary surgery followed by "high dose" CAP therapy [3].

High impact information on LNX1

• The mammalian numb phosphotyrosine-binding domain. Characterization of binding specificity and identification of a novel PDZ domain-containing numb binding protein, LNX [4].
• Finally, we also provide evidence that tyrosine phosphorylation of the LDNPAY sequence motif in LNX could generate a binding site for the phosphorylation-dependent binding of other PTB domain-containing proteins such as SHC [4].
• Experiments using dominant-negative constructs and RNA interference insure that Numb is necessary for the LNX1-mediated endocytosis of JAM4 [5].
• All these findings indicate that LNX1 provides an endocytic scaffold for JAM4 that is implicated in the reorganization of cell junctions [5].
• Ligand-of-Numb protein X1 facilitates endocytosis of JAM4 and is involved in transforming growth factor beta -induced redistribution of JAM4 in mammary epithelial cells [5].

Biological context of LNX1

• The presence of multiple protein binding domains involved in signal transduction and interaction with Numb and SKIP suggested an important role for LNX in tumorogenesis [1].
• Here we report the cloning of a novel 3.7-kb cDNA LNX from a human fetal brain cDNA library [6].
• By radiation hybrid mapping, we localize the LNX gene to human chromosome 4q12 between marker D4S1577 and marker D4S1594 [6].
• (c) Quantitative trait loci analyses in animals have identified that the Mpdz gene predisposes to alcohol dependence and withdrawal [7].

Anatomical context of LNX1

• Ligand-of-Numb protein X1 is expressed in kidney glomeruli and intestinal epithelial cells, where JAM4 is also detected [5].
• Two CAR-binding proteins belonging to the ligand-of-numb protein-X (LNX) family also occupied distinct regions in spermatozoa [8].

Associations of LNX1 with chemical compounds

• CAST and LNX were further colocalized with each other in a heterologous expression system, in which LNX was recruited to a Triton X-insoluble structure [9].

Physical interactions of LNX1

• It showed that human LNX interacted with Ski interacting protein (SKIP) via PDZ domains [1].

Other interactions of LNX1

• Junctional adhesion molecule 4, LNX1 and Numb form a tripartite complex in vitro and are partially colocalized in heterologous cells [5].
• LNX is the paralog of PDZRN1 (PDZ domain containing RING finger 1) [10].
• Ligand of Numb protein X (LNX) is PDZ domain containing protein that interacts with cell fate determinant Numb. cDNA microarray analysis was used to determine the expression of 13,939 genes in a set of 18 gliomas [1].

Analytical, diagnostic and therapeutic context of LNX1

• In situ hybridization analysis revealed that LNX was lowly expressed in cytoplasm of glioma cells [1].
• The co-immunoprecipitation results suggested that LNX interacted with SKIP in HEK293 cells [1].
• It showed that human LNX was downregulated in 100% of gliomas including low- and high-grade ones, which was confirmed by Northern blot [1].
• CONCLUSIONS: The results show that LNX might be of benefit in patients who have optimal primary cytoreductive surgery and who do not respond to platinum-based chemotherapy [2].
• Group C (n = 13) received TAH, BSO and OMTX at the primary operation and paraaortic and pelvic lymphadenectomy (LNX) at the second look operation (SLO) with "high dose" CAP therapy as did Group B [3].

References