Abstract
Numerous cell surface receptors and receptor-like proteins (RLPs) undergo activation or deactivation via a transmembrane domain (TMD). A subset of plant RLPs distinctively localizes to the plasma membrane-lined pores called plasmodesmata. Those RLPs include the Arabidopsis thaliana Plasmodesmata-located protein (PDLP) 5, which is well known for its vital function regulating plasmodesmal gating and molecular movement between cells. In this study, we report that the TMD, although not a determining factor for the plasmodesmal targeting, serves essential roles for the PDLP5 function. In addition to its role for membrane anchoring, the TMD mediates PDLP5 self-interaction and carries an evolutionarily conserved motif that is essential for PDLP5 to regulate cell-to-cell movement. Computational modeling-based analyses suggest that PDLP TMDs have high propensities to dimerize. We discuss how a specific mode(s) of TMD dimerization might serve as a common mechanism for PDLP5 and other PDLP members to regulate cell-to-cell movement.
Highlights
Numerous cell surface receptors and receptor-like proteins (RLPs) undergo activation or deactivation via a transmembrane domain (TMD)
For the multiple sequence comparison, a total of 491 entries were chosen from UniProtKB for our analysis
We have found that the PDLP5 TMD sequence was replaceable with different TMD sequences without affecting plasmodesmal localization
Summary
Numerous cell surface receptors and receptor-like proteins (RLPs) undergo activation or deactivation via a transmembrane domain (TMD). A subset of plant RLPs distinctively localizes to the plasma membrane-lined pores called plasmodesmata Those RLPs include the Arabidopsis thaliana Plasmodesmata-located protein (PDLP) 5, which is well known for its vital function regulating plasmodesmal gating and molecular movement between cells. Plasmodesmata are membrane-lined cytoplasmic nanochannels through which various molecules move between cells Soluble molecules such as small nutrients, hormones, and ions, move by simple diffusion, whereas some specialized macromolecules through active transport. We have previously shown that the Arabidopsis thaliana Plasmodesmata-located protein (PDLP) 5 localizes to the central region of plasmodesmata and functions as a potent inhibitor of molecular movement between cells[3,4]. A recent structural study using heterologously expressed DUF26, derived from PDLP5 and PDLP8 ExD sequences, revealed that they each form intramolecular disulfide bonds and fold to Gnk[212]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
