Interaction with COPII Member SAR1 Is Critical for the Delivery of

Ning Zhang, Jordan D Julian, Olga A Zabotina

Abstract read

In one paragraph

Article in Plants (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

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0 citing papers in PubMed.

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5 · Who and what money

Authors and funding

3 authors.

Ning ZhangRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.ORCID 0000-0002-4211-9865

Jordan D JulianRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.ORCID 0009-0002-7204-9957

Olga A ZabotinaRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.ORCID 0000-0001-6938-6923

Funding

U.S. National Science Foundation Division of Molecular and Cellular Biosciences 1856477

6 · The paper itself

Abstract

Transport of Golgi-localized proteins from the ER is mediated by the coat protein complex II (COPII) and its members, COPII inner coat subunit Sec24 and Secretion-associated Ras-related GTPase 1 (Sar1). Sar1 and Sec24 recognize cytosolic N-termini of glycosyltransferases (GTs) that contain peptide signals required for incorporation into COPII-coated vesicles. Xyloglucan Xylosyltransferases (XXTs) are required for xyloglucan (XyGs) biosynthesis and must be transported to the Golgi for proper function. In this study, we demonstrated that XXTs interact with AtSar1 in the COPII complex but not with AtSec24, which was previously reported to be the main recruiter of cargo proteins into COPII-coated vesicles. The mutation of the arginine to glutamine residues of di-arginine motifs in the N-termini of XXTs caused protein mislocalization and significantly reduced the strength of the interaction with AtSar1. These mutations caused 90% of XXTs to either remain in the ER or localize to small non-Golgi compartments. In turn, such mislocalization significantly suppressed the recovery of XyGs biosynthesis in

Indexed as

AtSar1 proteincargo selection by COPII complexprotein traffickingxyloglucan biosynthesisXyloglucan Xylosyltransferases

Identifiers

PMID41829853

DOI10.3390/plants15050822

PMCPMC12986673

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