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ProteomicsIdentification of MARCH2 E3 ligase-substrates using proximity-dependent biotin labeling method
MARCH2 is known to be involved in intracellular vesicular trafficking. To identify its substrates, we have recently developed a method based on proximity-dependent biotin labelling. In this protocol, the MARCH2 ubiquitin ligase of interest is expressed as a fusion to Escherichia coli biotin ligase ...
ORGANISM(S): Homo sapiens (Human) 
2019-06-06 | PXD013601 | Pride
March2 Secretory proteins E3 ligase 
UnknownMARCH2 suppresses odontoblast differentiation by polyubiquitinating PTPRD.
Not available
S-EPMC12789588 | biostudies-literature
UnknownDetermining the antiviral mechanism of MARCH2.
Not available
S-EPMC10541590 | biostudies-literature
UnknownThe E3 ubiquitin ligase MARCH2 controls TNF-α mediated inflammation by autoubiquitination.
Not available
S-EPMC12126869 | biostudies-literature
UnknownNegative regulation of NEMO signaling by the ubiquitin E3 ligase MARCH2.
Not available
S-EPMC7604578 | biostudies-literature
UnknownMARCH2, a T cell specific factor that restricts HIV-1 infection.
Not available
S-EPMC11309421 | biostudies-literature
UnknownThe E3 ubiquitin ligase MARCH2 regulates ERGIC3-dependent trafficking of secretory proteins.
Not available
S-EPMC6635435 | biostudies-literature
UnknownMARCH2 regulates autophagy by promoting CFTR ubiquitination and degradation and PIK3CA-AKT-MTOR signaling.
Not available
S-EPMC5082784 | biostudies-literature
UnknownMARCH2, a Novel Oncogene-regulated SNAIL E3 Ligase, Suppresses Triple-negative Breast Cancer Metastases.
Not available
S-EPMC10977041 | biostudies-literature
UnknownDLG1 is an anchor for the E3 ligase MARCH2 at sites of cell-cell contact.
Not available
S-EPMC2257480 | biostudies-literature
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