scholarly journals Functional Diversification of B MADS-Box Homeotic Regulators of Flower Development: Adaptive Evolution in Protein–Protein Interaction Domains after Major Gene Duplication Events

2006 ◽  
Vol 24 (2) ◽  
pp. 465-481 ◽  
Author(s):  
Tania Hernández-Hernández ◽  
León Patricio Martínez-Castilla ◽  
Elena R. Alvarez-Buylla
Keyword(s):  
Gene Duplication ◽  
Adaptive Evolution ◽  
Protein Interaction ◽  
Flower Development ◽  
Major Gene ◽  
Mads Box ◽  
Functional Diversification ◽  
Protein Protein Interaction ◽  
Duplication Events ◽  
Interaction Domains

scholarly journals Orchid Bsister gene PeMADS28 displays conserved function in ovule integument development

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Ching-Yu Shen ◽  
You-Yi Chen ◽  
Ke-Wei Liu ◽  
Hsiang-Chia Lu ◽  
Song-Bin Chang ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Protein Interaction ◽  
Ectopic Expression ◽  
Flowering Plants ◽  
Complementation Test ◽  
Ovule Development ◽  
Mads Box ◽  
Temporal Expression ◽  
Protein Protein Interaction ◽  
Silique Length

AbstractThe ovules and egg cells are well developed to be fertilized at anthesis in many flowering plants. However, ovule development is triggered by pollination in most orchids. In this study, we characterized the function of a Bsister gene, named PeMADS28, isolated from Phalaenopsis equestris, the genome-sequenced orchid. Spatial and temporal expression analysis showed PeMADS28 predominantly expressed in ovules between 32 and 48 days after pollination, which synchronizes with integument development. Subcellular localization and protein–protein interaction analyses revealed that PeMADS28 could form a homodimer as well as heterodimers with D-class and E-class MADS-box proteins. In addition, ectopic expression of PeMADS28 in Arabidopsis thaliana induced small curled rosette leaves, short silique length and few seeds, similar to that with overexpression of other species’ Bsister genes in Arabidopsis. Furthermore, complementation test revealed that PeMADS28 could rescue the phenotype of the ABS/TT16 mutant. Together, these results indicate the conserved function of BsisterPeMADS28 associated with ovule integument development in orchid.

scholarly journals Mutations and Protein Interaction Landscape Reveal Key Cellular Events Perturbed in Upper Motor Neurons with HSP and PLS

2021 ◽  
Vol 11 (5) ◽  
pp. 578
Author(s):  
Oge Gozutok ◽  
Benjamin Ryan Helmold ◽  
P. Hande Ozdinler
Keyword(s):  
Motor Neurons ◽  
Protein Interaction ◽  
Protein Interactions ◽  
Cortical Neurons ◽  
Therapeutic Interventions ◽  
Functional Identification ◽  
Protein Protein Interaction ◽  
Cellular Events ◽  
Interaction Domains ◽  
Upper Motor Neurons

Hereditary spastic paraplegia (HSP) and primary lateral sclerosis (PLS) are rare motor neuron diseases, which affect mostly the upper motor neurons (UMNs) in patients. The UMNs display early vulnerability and progressive degeneration, while other cortical neurons mostly remain functional. Identification of numerous mutations either directly linked or associated with HSP and PLS begins to reveal the genetic component of UMN diseases. Since each of these mutations are identified on genes that code for a protein, and because cellular functions mostly depend on protein-protein interactions, we hypothesized that the mutations detected in patients and the alterations in protein interaction domains would hold the key to unravel the underlying causes of their vulnerability. In an effort to bring a mechanistic insight, we utilized computational analyses to identify interaction partners of proteins and developed the protein-protein interaction landscape with respect to HSP and PLS. Protein-protein interaction domains, upstream regulators and canonical pathways begin to highlight key cellular events. Here we report that proteins involved in maintaining lipid homeostasis and cytoarchitectural dynamics and their interactions are of great importance for UMN health and stability. Their perturbation may result in neuronal vulnerability, and thus maintaining their balance could offer therapeutic interventions.

Patterns of gene duplication and functional diversification during the evolution of the AP1/SQUA subfamily of plant MADS-box genes

2007 ◽  
Vol 44 (1) ◽  
pp. 26-41 ◽  
Author(s):  
Hongyan Shan ◽  
Ning Zhang ◽  
Cuijing Liu ◽  
Guixia Xu ◽  
Jian Zhang ◽  
...  
Keyword(s):  
Gene Duplication ◽  
Mads Box ◽  
Mads Box Genes ◽  
Functional Diversification

scholarly journals Impacts of protein-protein interaction domains on organism and network complexity

2008 ◽  
Vol 18 (9) ◽  
pp. 1500-1508 ◽  
Author(s):  
K. Xia ◽  
Z. Fu ◽  
L. Hou ◽  
J.-D. J. Han
Keyword(s):  
Protein Interaction ◽  
Protein Protein Interaction ◽  
Interaction Domains

Recognition of Proline-Rich Motifs by Protein-Protein-Interaction Domains

2005 ◽  
Vol 44 (19) ◽  
pp. 2852-2869 ◽  
Author(s):  
Linda J. Ball ◽  
Ronald Kühne ◽  
Jens Schneider-Mergener ◽  
Hartmut Oschkinat
Keyword(s):  
Protein Interaction ◽  
Protein Protein Interaction ◽  
Interaction Domains

scholarly journals LRRK2 GTPase dysfunction in the pathogenesis of Parkinson's disease

2012 ◽  
Vol 40 (5) ◽  
pp. 1074-1079 ◽  
Author(s):  
Yulan Xiong ◽  
Valina L. Dawson ◽  
Ted M. Dawson
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Protein Interaction ◽  
Kinase Activity ◽  
Present Review ◽  
Signalling Pathways ◽  
Gtpase Activity ◽  
Leucine Rich Repeat ◽  
Protein Protein Interaction ◽  
Interaction Domains

Mutations in the LRRK2 (leucine-rich repeat kinase 2) gene are the most frequent genetic cause of PD (Parkinson's disease), and these mutations play important roles in sporadic PD. The LRRK2 protein contains GTPase and kinase domains and several protein–protein interaction domains. The kinase and GTPase activity of LRRK2 seem to be important in regulating LRRK2-dependent cellular signalling pathways. LRRK2's GTPase and kinase domains may reciprocally regulate each other to direct LRRK2's ultimate function. Although most LRRK2 investigations are centred on LRRK2's kinase activity, the present review focuses on the function of LRRK2's GTPase activity in LRRK2 physiology and pathophysiology.

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