ArticleMolecular biology reports2010
LNX (Ligand of Numb-protein X) interacts with RhoC, both of which regulate AP-1-mediated transcriptional activation.
Article in Molecular biology reports, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Activation of RhoC by regulatory ubiquitination is mediated by LNX1 and suppressed by LIS1.Scientific reports · 2022Article
- LNX1/LNX2 proteins: functions in neuronal signalling and beyond.Neuronal signaling · 2018Review
- Gene polymorphisms and oral cancer risk in tobacco habitués.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- The Roles of RNase-L in Antimicrobial Immunity and the Cytoskeleton-Associated Innate Response.International journal of molecular sciences · 2016Review
- Role of Numb expression and nuclear translocation in endometrial cancer.Oncology letters · 2015Article
- A new mechanism of RhoA ubiquitination and degradation: roles of SCF(FBXL19) E3 ligase and Erk2.Biochimica et biophysica acta · 2013Article
- Molecular evolution of the LNX gene family.BMC evolutionary biology · 2011Article
- Ubiquitination: Added complexity in Ras and Rho family GTPase function.Small GTPases · 2011Article
- Article
- MYBBP1A: a new Ipr1's binding protein in mice.Molecular biology reports · 2010Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LNX (Ligand of Numb-protein X) was originally isolated as a binding partner to the cell-fate Determinant Numb during development, and then identified to act as a RING finger-type E3 ubiquitin ligase for the ubiquitylation and degradation of Numb. LNX contains 4 PDZ domains which are proved to play a central role in organizing diverse cell signaling assemblies. A yeast two-hybrid screening was used to identify LNX as a potential binding partner for RhoC. RhoC, a member of the Ras family of small GTPases, promotes reorganization of the actin cytoskeleton and regulation of cell shape, attachment, and motility. The interaction between LNX and RhoC in mammalian cells was identified by co-immunoprecipitation assays, and the efficient binding required the first PDZ domain of LNX. LNX and RhoC were further colocalized with each other in mammalian cells, in which RhoC changed its sublocalization from cytoplasm to nucleus when co-transferred with LNX. Furthermore, co-expression of RhoC reduced the transcriptional activity of AP-1, which was up-regulated by over-expression of LNX alone. These results suggest that LNX and RhoC might be part of a larger protein complex that would have important functions in signaling transduction about regulating the transcriptional activities of AP-1.
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