scholarly journals A Dual Mechanism Controls Nuclear Localization in the Atypical Basic-Helix-Loop-Helix Protein PAR1 of Arabidopsis thaliana

2012 ◽  
Vol 5 (3) ◽  
pp. 669-677 ◽  
Author(s):  
Anahit Galstyan ◽  
Jordi Bou-Torrent ◽  
Irma Roig-Villanova ◽  
Jaime F. Martínez-García
2004 ◽  
Vol 16 (11) ◽  
pp. 3045-3058 ◽  
Author(s):  
Eunkyoo Oh ◽  
Jonghyun Kim ◽  
Eunae Park ◽  
Jeong-Il Kim ◽  
Changwon Kang ◽  
...  

Development ◽  
1994 ◽  
Vol 120 (9) ◽  
pp. 2385-2396 ◽  
Author(s):  
R. Kopan ◽  
J.S. Nye ◽  
H. Weintraub

We show that Myf-5 and mNotch mRNA are both present in the presomitic mesoderm before muscle cell commitment and before muscle structural gene activation. The failure of presomitic mesoderm to respond to Myf-5 and express myogenic properties implies that there may be a mechanism in presomitic mesoderm to suppress muscle differentiation. Here we show that ectopic expression of the intracellular domain of mNotch (mNotchIC) functions as a constitutively activated repressor of myogenesis both in cultured cells and in frog embryos. Mutagenesis experiments indicate that the target for inactivation by mNotch is the MyoD basic helix-loop-helix domain. mNotchIC contains a nuclear localization signal and localizes to the nucleus. Removal of the nuclear localization signal (NLS) reduces nuclear localization and diminishes the inhibition of myogenesis caused by Myf-5 or MyoD. Additional experiments show that the CDC10/SWI6/ankyrin repeats are also necessary for myogenic inhibition.


2001 ◽  
Vol 20 (8) ◽  
pp. 465-471 ◽  
Author(s):  
Jerelyn Wong ◽  
Melanie Funes-Duran ◽  
Jessica Ahlberg ◽  
June Round ◽  
Ryan O'Connell ◽  
...  

2018 ◽  
Vol 132 (1) ◽  
pp. 93-105 ◽  
Author(s):  
Noriaki Tanabe ◽  
Masahiro Noshi ◽  
Daisuke Mori ◽  
Kotaro Nozawa ◽  
Masahiro Tamoi ◽  
...  

2019 ◽  
Vol 48 (2) ◽  
pp. 934-948 ◽  
Author(s):  
Vivian Pogenberg ◽  
Josué Ballesteros-Álvarez ◽  
Romana Schober ◽  
Ingibjörg Sigvaldadóttir ◽  
Agnieszka Obarska-Kosinska ◽  
...  

Abstract Interrupted dimeric coiled coil segments are found in a broad range of proteins and generally confer selective functional properties such as binding to specific ligands. However, there is only one documented case of a basic-helix–loop–helix leucine zipper transcription factor—microphthalmia-associated transcription factor (MITF)—in which an insertion of a three-residue stammer serves as a determinant of conditional partner selectivity. To unravel the molecular principles of this selectivity, we have analyzed the high-resolution structures of stammer-containing MITF and an engineered stammer-less MITF variant, which comprises an uninterrupted symmetric coiled coil. Despite this fundamental difference, both MITF structures reveal identical flanking in-phase coiled coil arrangements, gained by helical over-winding and local asymmetry in wild-type MITF across the stammer region. These conserved structural properties allow the maintenance of a proper functional readout in terms of nuclear localization and binding to specific DNA-response motifs regardless of the presence of the stammer. By contrast, MITF heterodimer formation with other bHLH-Zip transcription factors is only permissive when both factors contain either the same type of inserted stammer or no insert. Our data illustrate a unique principle of conditional partner selectivity within the wide arsenal of transcription factors with specific partner-dependent functional readouts.


2003 ◽  
Vol 15 (11) ◽  
pp. 2497-2502 ◽  
Author(s):  
Paul C. Bailey ◽  
Cathie Martin ◽  
Gabriela Toledo-Ortiz ◽  
Peter H. Quail ◽  
Enamul Huq ◽  
...  

2020 ◽  
Author(s):  
Sandi Paulišić ◽  
Christiane Then ◽  
Benjamin Alary ◽  
Fabien Nogue ◽  
Miltos Tsiantis ◽  
...  

ABSTRACTShade caused by the proximity of neighboring vegetation triggers a set of acclimation responses to either avoid or tolerate shade. Comparative analyses between the shade avoider Arabidopsis thaliana and the shade tolerant Cardamine hirsuta, revealed a role for the atypical basic-helix-loop-helix LONG HYPOCOTYL IN FR 1 (HFR1) in maintaining the shade-tolerance in C. hirsuta, inhibiting hypocotyl elongation in shade and constraining expression profile of shade induced genes. We showed that C. hirsuta HFR1 protein is more stable than its A. thaliana counterpart, contributing to enhance its biological activity. The enhanced HFR1 activity is accompanied by an attenuated PHYTOCHROME INTERACTING FACTOR (PIF) activity in C. hirsuta. As a result, the PIF-HFR1 module is imbalanced, causing a reduced PIF activity and attenuating other PIF-mediated responses such as warm temperature-induced hypocotyl elongation (thermomorphogenesis) and dark-induced senescence. By this mechanism and that of the already-known of phytochrome A photoreceptor, plants might ensure to properly adapt and thrive in habitats with disparate light amounts.


Sign in / Sign up

Export Citation Format

Share Document