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STAMBP deubiquitinates NLRP7. 9 / 9
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"Moreover, complex post-translational modifications regulate its activity; namely, NLRP7 is either ubiquitinated to regulate its functions, or deubiquitinated by the STAM-binding protein to prevent its trafficking to lysosomes and its degradation [59]."

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"BC-1471 (43) was discovered as a specific STAMBP inhibitor (IC 50 = 0.33 muM) that selectively blocked deubiquitination of Ub-NALP7 by recombinant STAMBP [XREF_BIBR] but did not significantly inhibit the activity of a panel of 38 different DUBs at the concentration tested."

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"Our findings suggest that STAMBP (STAM binding protein), which deubiquitinates NALP7 and increases its abundance by preventing lysosomal trafficking, may promote inflammatory factors ."

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"Since STAMBP is known to function as a DUB, we developed a cell-free DUB assay to test STAMBP deubiquitination of NALP7."

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"This finding supports that STAMBP is sufficient to directly deubiquitinate NALP7."

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"We next tested inhibition of STAMBP DUB activity specific to Ub-NALP7; here inclusion of BC-1471 blocked STAMBP mediated deubiquitination of Ub-NALP7 in vitro in a concentration dependent manner (XREF_FIG), where BC-1471 performed comparably to the broad-spectrum metalloprotease DUB inhibitor 1,10-phenanthroline."

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"STAMBP is sufficient to deubiquitinate NALP7 and is necessary to stabilize NALP7 protein in cells exposed to LPS or Pam3CSK4."

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"Bednash et al. 75 showed that the DUB STAMPBP (or AMSH) deubiquitinates NLRP7 rescuing this receptor from progressing to lysosome degradation and making it available for the formation of an active inflammasome."

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"STAMBP promotes inflammasome activity in innate immune responses by mediating the deubiquitination of NALP7 and preventing the transport of NALP7 to lysosomes, thereby increasing NALP7 abundance ."