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Significance Defects in systems that orchestrate the intracellular clearance of misfolded proteins are implicated as central contributors to numerous human diseases. Our study has further elucidated the unexpected capacity for the prototype mannosidase, Man1b1, to target misfolded alpha1-antitrypsin for intracellular loss by an unconventional, N-glycan-independent manner. Identification of this functional dichotomy, and especially the Man1b1-mediated catalysis-independent system, might influence the design of future therapeutic interventions for selected conformational diseases of the secretory pathway.

The cytoplasmic tail of human mannosidase Man1b1 contributes to catalysis-independent quality control of misfolded alpha1-antitrypsin