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MARCH1 is a member of the MARCH family of membrane-bound E3 ubiquitin ligases (EC 220.127.116.11). Additionally we are shipping MARCH1 Proteins (4) and many more products for this protein.
Showing 10 out of 48 products:
Human Polyclonal MARCH1 Primary Antibody for ELISA - ABIN548211
Matsuki, Ohmura-Hoshino, Goto, Aoki, Mito-Yoshida, Uematsu, Hasegawa, Koseki, Ohara, Nakayama, Toyooka, Matsuoka, Hotta, Yamamoto, Ishido: Novel regulation of MHC class II function in B cells. in The EMBO journal 2007
found downstream sequence elements, present in the first coding exon of March-I in antigen-presenting cells (APCs), that confer regulation of March-I expression in activated APCs
March-I undergoes lysine-independent ubiquitination by an as yet unidentified E3 ubiquitin ligase that, together with Ube2D1, regulates March-I expression
MARCH1 ubiquitinates INSR to decrease cell surface INSR levels, but unlike other INSR ubiquitin ligases, MARCH1 acts in the basal state rather than after insulin stimulation.
MARCH1 functions as a tumor promoter by upregulating the NF-kappaB and the Wnt/b-catenin pathways, indicating that MARCH1 may be a therapeutic target for patients with ovarian cancer.
findings highlight the complex regulation of MARCH1 trafficking in the endocytic pathway as well as the intricate interactions between its cytoplasmic tails.
MARCH1 is capable of autoubiquitination, thus regulating its own expression.
expression of MARCH1 or MARCH8 causes a drastic change CD98 trafficking after endocytosis
MARCH I is a major regulator of HLA-DR traffic, and its loss contributes to the acquisition of the potent immunostimulatory properties of mature human DCs.
The immunosuppressive effect of IL-10 on antigen presentation is mediated through induced expression of MARCH1.
unexpected intersection between MHC I and MHC II such that the surface expression of both molecules are indirectly and directly regulated by MARCH1 ubiquitination, respectively.
Study shows march1-dependent modulation of donor MHC II on CD103(+) dendritic cells mitigates alloimmunity
these results demonstrate a role of March1 E3 ubiquitin ligase in modulating allergic responses
March1 loss-of-function enhances, and March1 overexpression impairs, hepatic insulin sensitivity in mice.
We conclude that MARCH1 exerts MHCII-independent effects that regulate the innate arm of immunity
March-I ubiquitination prevents MHC class II recycling and promotes MHC class II turnover in antigen-presenting cells
IL-10 stimulates expression of the E3 ubiquitin ligase March-I in activated macrophages, thereby down-regulating MHC-II, CD86, and antigen presentation to CD4 T cells.
Dendritic cells co-cultivated with antigen-specific induced Tregs expressed high levels of MARCH1. A major suppressive mechanism of DC function by iTregs is secondary to the effects of IL-10 on MARCH1 & CD83 expression.
DCs deficient in MARCH1 or MHCII ubiquitination both failed to generate antigen-specific T reg cells in vivo and in vitro.
aberrant degradation of spleen DCs MARCH1-mediated ubiquitinated proteins is involved during the earliest stage of MODS development.
IL-10 can have opposite effects on MARCH1 regulation in different cell types.
Ubiquitin-mediated regulation of CD86 protein expression by the ubiquitin ligase membrane-associated RING-CH-1 (MARCH1).
found that the transmembrane domain of CD83 enhances MHC class II and CD86 expression by blocking MHC class II association with the ubiquitin ligase MARCH1
Selective ubiquitination of MHC-II in immature dendritic cells by the E3 ubiquitin ligase March-I results in the selective degradation of internalized pMHC-II.
The function of MHC II in B cells is regulated through ubiquitination by MARCH-I.
MARCH1 expression is regulated at a posttranscriptional level by trafficking within the endolysosomal pathway where MARCH1 is proteolyzed.
MARCH-I may function as a housekeeper of conventional dendritic cell in the steady state.
Study demonstrated the significant associations of genetic variants of the PDGFRB and MARCH1 genes with semen production traits.
MARCH1 is a member of the MARCH family of membrane-bound E3 ubiquitin ligases (EC 18.104.22.168). MARCH proteins add ubiquitin (see MIM 191339) to target lysines in substrate proteins, thereby signaling their vesicular transport between membrane compartments. MARCH1 downregulates the surface expression of major histocompatibility complex (MHC) class II molecules (see MIM 142880) and other glycoproteins by directing them to the late endosomal/lysosomal compartment (Bartee et al., 2004
E3 ubiquitin-protein ligase MARCH1
, RING finger protein 171
, membrane-associated RING finger protein 1
, membrane-associated RING-CH protein I
, membrane-associated ring finger (C3HC4) 1