Are cuproproteins part of the multi-protein framework for making the Casparian strip?

Abstract

Casparian strip (CS) is a lignified structure localized on the cell wall between adjacent root endodermal cells and functions as an apoplastic diffusion barrier in the root. The polarly localized, lignin-based CS is an excellent system for studying peptide signaling and position recognition. In this short review, we summarize advances in the past decade on the molecular mechanism governing CS development. In addition to the multi-protein framework underlying the CS membrane domain, we discuss recently observed participation of cell wall located cuproproteins in CS formation. These new discoveries shed light on a potential CS wall domain that coordinates with the membrane domain to provide bidirectional positional information for guiding precise CS development.

Proteomic Analysis: Explosive Salt Accumulation in Leaves of Morus alba L. under Salt Stress

“…Distribution of CASPs in EXO70A1 mutant strains tends to be randomized. At the same time, LAC3 and UCC1 were located at the boundary and central microregion of the CS formation area, respectively, guiding the fixed-point deposition of the lignin [74]. The expression of EXO70B1 was down-regulated with the increase of salt stress, and the expression of UCC1 remained stable under R3 but fell by about 80% in R4.…”

The Copper Responsive Transcription Factor SPL7 Represses Key Abscisic Acid Biosynthetic Genes to Balance Growth and Drought Tolerance

“…Copper (Cu) is a trace transition metal in plants that serves as the cofactor for cuproproteins with vital electron transfer or redox reaction functions (Burkhead et al, 2009; Peñarrubia et al, 2015; Zhuang and Li, 2020). In higher plants, Cu is required for growth because the small blue Cu protein plastocyanin, abundantly present in the thylakoid lumen, is an indispensable electron carrier in the Z-scheme of photosynthesis (Molina-Heredia et al, 2003; Weigel et al, 2003).…”