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

Ashlee H. Sun | Zendy; John R. Collette | Zendy; Richard N. Sifers | Zendy

Open Access

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

Author(s) -

Ashlee H. Sun,

John R. Collette,

Richard N. Sifers

Publication year - 2020

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.1919013117

Subject(s) - intracellular , glycan , cytoplasm , mannosidase , protein folding , microbiology and biotechnology , biology , identification (biology) , chemistry , biochemistry , computational biology , enzyme , glycoprotein , botany

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.

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