title: CELLULOSE SYNTHASE INTERACTIVE1 Is Required for Fast Recycling of Cellulose Synthase Complexes to the Plasma Membrane in Arabidopsis.
abstract: Plants are constantly subjected to various biotic and abiotic stresses and have evolved complex strategies to cope with these stresses. For example, plant cells endocytose plasma membrane material under stress and subsequently recycle it back when the stress conditions are relieved. Cellulose biosynthesis is a tightly regulated process that is performed by plasma membrane-localized cellulose synthase (CESA) complexes (CSCs). However, the regulatory mechanism of cellulose biosynthesis under abiotic stress has not been well explored. In this study, we show that small CESA compartments (SmaCCs) or microtubule-associated cellulose synthase compartments (MASCs) are critical for fast recovery of CSCs to the plasma membrane after stress is relieved in Arabidopsis thaliana. This SmaCC/MASC-mediated fast recovery of CSCs is dependent on CELLULOSE SYNTHASE INTERACTIVE1 (CSI1), a protein previously known to represent the link between CSCs and cortical microtubules. Independently, AP2M, a core component in clathrin-mediated endocytosis, plays a role in the formation of SmaCCs/MASCs. Together, our study establishes a model in which CSI1-dependent SmaCCs/MASCs are formed through a process that involves endocytosis, which represents an important mechanism for plants to quickly regulate cellulose synthesis under abiotic stress.
authors.affiliation: Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802.
authors.forename: Lei
authors.initials: L
authors.lastname: Lei
authors.affiliation: Department of Materials Science and Engineering, North Carolina State University, Raleigh, North Carolina 27695.
authors.forename: Abhishek
authors.identifier: http://orcid.org/0000-0002-9450-7229
authors.initials: A
authors.lastname: Singh
authors.affiliation: Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802.
authors.forename: Logan
authors.initials: L
authors.lastname: Bashline
authors.affiliation: Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802.
authors.forename: Shundai
authors.initials: S
authors.lastname: Li
authors.affiliation: Department of Materials Science and Engineering, North Carolina State University, Raleigh, North Carolina 27695.
authors.forename: Yaroslava G
authors.identifier: http://orcid.org/0000-0002-8557-9992
authors.initials: YG
authors.lastname: Yingling
authors.affiliation: Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802 yug13@psu.edu.
authors.forename: Ying
authors.identifier: http://orcid.org/0000-0001-8415-4768
authors.initials: Y
authors.lastname: Gu
mesh_terms: D017360:Arabidopsis / Q000235:genetics* / Q000502:physiology / Q000648:ultrastructure; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D002482:Cellulose / Q000378:metabolism*; D002966:Clathrin / Q000378:metabolism; D004705:Endocytosis; D017930:Genes, Reporter; D005964:Glucosyltransferases / Q000235:genetics / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism; D008958:Models, Molecular; D021381:Protein Transport; D036226:Seedlings / Q000235:genetics / Q000502:physiology / Q000648:ultrastructure
chemical_list: D029681:Arabidopsis Proteins; C551801:CSI1 protein, Arabidopsis; D002352:Carrier Proteins; D002966:Clathrin; D002482:Cellulose; D005964:Glucosyltransferases; C478648:cellulose synthase