14-3-3 proteins contribute to leaf and root development via brassinosteroid insensitive 1 in Arabidopsis thaliana
Background Brassinosteroids (BR) are essential growth hormone in plants. Various components involved in signal transduction pathway have been identified as targets of 14-3-3 phospho-binding proteins. Previously, we showed that 14-3-3 proteins directly interact with the Brassinosteroid Insensitive 1...
Saved in:
Published in | Genes & genomics Vol. 42; no. 3; pp. 347 - 354 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Singapore
Springer Singapore
01.03.2020
Springer Nature B.V 한국유전학회 |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | Background
Brassinosteroids (BR) are essential growth hormone in plants. Various components involved in signal transduction pathway have been identified as targets of 14-3-3 phospho-binding proteins. Previously, we showed that 14-3-3 proteins directly interact with the Brassinosteroid Insensitive 1 (BRI1), the BR receptor kinase, and are also subject to phosphorylation in a BR-dependent manner.
Objective
In this study, we aimed to examine a potential interplay between 14-3-3 proteins and BRI1 in plant growth.
Methods
Morphological phenotypes of a T-DNA insertion mutant line,
14
-
3
-
3ψφε
, defective in three 14-3-3 isoforms, psi, phi and epsilon, were characterized and compared with
bri1
-
5
and two transgenic lines for BRI1, BRI1-Flag and BRI1-Flag (
14
-
3
-
3ψφε
). We also generated complementation lines carrying each of the three 14-3-3 genes and determined their differences in rosette growth.
Results
No significant differences between the wild-type and
14
-
3
-
3ψφε
seedlings were observed regardless of BR applications. However, BRI1-Flag (
14
-
3
-
3ψφε
) showed a significantly reduced cold tolerance and BR sensitivity in hypocotyl and root development when compared to BRI1-Flag. In addition, narrower leaf shape and smaller rosette size were observed in BRI1-Flag (
14
-
3
-
3ψφε
), while the mutant phenotypes were partially restored in the complementation lines, two of which with
14
-
3
-
3φ
and
14
-
3
-
3ε
showed the rosette growth comparable to BRI1-Flag.
Conclusion
Taken together, our results suggested that 14-3-3 proteins might positively regulate BRI1 activity and showed that 14-3-3 isoforms have different functional impacts in BR signaling. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
ISSN: | 1976-9571 2092-9293 2092-9293 |
DOI: | 10.1007/s13258-019-00909-4 |