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LRSAM1 encodes a ring finger protein involved in a variety of functions, including regulation of signaling pathways and cell adhesion, mediation of self-ubiquitylation, and involvement in cargo sorting during receptor endocytosis. Zusätzlich bieten wir Ihnen LRSAM1 Antikörper (57) und LRSAM1 Kits (4) und viele weitere Produktgruppen zu diesem Protein an.
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We identified a novel LRSAM1 missense mutation (c.2120C > T, p.Pro707Leu) mapping to the RING domain. The identified missense mutation, as well as of another recently reported pathogenic missense mutation (c.2081G > A, p.Cys694Tyr), revealed that in vitro ubiquitylation activity was largely abrogated.
findings suggest that the mutant LRSAM1 may aberrantly affect the formation of transcription machinery.
findings demonstrate that the isolated genetic entity Charcot-Marie-Tooth type 2G is caused by a missense mutation in LRSAM1.
LRSAM1 exhibited self-association in vitro and in vivo. The study found the self-association of LRSAM1 promotes intermolecular ubiquitination and proved a potential N-terminal ubiquitination.
Plant homeodomain finger protein 23 negatively regulates cell autophagy by promoting ubiquitination and degradation of E3 ligase LRSAM1
disruption of the C-terminal RING domain confers dominant negative properties to LRSAM1
Our data further confirms that LRSAM1 mutations are associated with CMT2 of AD inheritance.
Authors identify LRSAM1 as the E3 ligase responsible for anti-Salmonella autophagy-associated ubiquitination.
homozygous mutation in LRSAM1 was proposed as a strong candidate for the disease in a family with recessive axonal polyneuropathy
LRSAM1 as a component of the antibacterial autophagic response.
LRSAM1 is a strong candidate for the causal gene for the Charcot-Marie-Tooth disease.
Results suggest that RIFLE represents a novel signaling protein that mediates components of the Wnt/wingless signaling pathway and cell adhesion in PC12 cells [RIFLE protein].
Tal regulates a Tsg101-associated complex responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the multivesicular body and at the plasma membrane
Tal polyubiquitinates lysine residues in the C-terminus of uncomplexed Tsg101, resulting in proteasomal degradation.
This gene encodes a ring finger protein involved in a variety of functions, including regulation of signaling pathways and cell adhesion, mediation of self-ubiquitylation, and involvement in cargo sorting during receptor endocytosis. Mutations in this gene have been associated with Charcot-Marie-Tooth disease. Multiple transcript variants encoding different isoforms have been identified for this gene.
E3 ubiquitin-protein ligase LRSAM1
, Tsg101-associated ligase
, leucine-rich repeat and sterile alpha motif-containing protein 1
, tsg101-associated ligase