BRL1, a leucine‐rich repeat receptor‐like protein kinase, is functionally redundant with BRI1 in regulating Arabidopsis brassinosteroid signaling

2004 ◽  
Vol 40 (3) ◽  
pp. 399-409 ◽  
Author(s):  
Aifen Zhou ◽  
Huachun Wang ◽  
John C. Walker ◽  
Jia Li
Keyword(s):  
Protein Kinase ◽  
Leucine Rich Repeat ◽  
Brassinosteroid Signaling

Biochemical and functional characterization of the ROC domain of DAPK establishes a new paradigm of GTP regulation in ROCO proteins

2012 ◽  
Vol 40 (5) ◽  
pp. 1052-1057 ◽  
Author(s):  
Shani Bialik ◽  
Adi Kimchi
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Functional Characterization ◽  
Leucine Rich Repeat ◽  
New Paradigm ◽  
Gtp Binding ◽  
Death Associated Protein Kinase ◽  
In Cis ◽  
Leucine Rich Repeat Protein

DAPK (death-associated protein kinase) is a newly recognized member of the mammalian family of ROCO proteins, characterized by common ROC (Ras of complex proteins) and COR (C-terminal of ROC) domains. In the present paper, we review our recent work showing that DAPK is functionally a ROCO protein; its ROC domain binds and hydrolyses GTP. Furthermore, GTP binding regulates DAPK catalytic activity in a novel manner by enhancing autophosphorylation on inhibitory Ser308, thereby promoting the kinase ‘off’ state. This is a novel mechanism for in cis regulation of kinase activity by the distal ROC domain. The functional similarities between DAPK and the Parkinson's disease-associated protein LRRK2 (leucine-rich repeat protein kinase 2), another member of the ROCO family, are also discussed.

scholarly journals Origin and diversification of leucine-rich repeat receptor-like protein kinase (LRR-RLK) genes in plants

2017 ◽  
Vol 17 (1) ◽  
Author(s):  
Ping-Li Liu ◽  
Liang Du ◽  
Yuan Huang ◽  
Shu-Min Gao ◽  
Meng Yu
Keyword(s):  
Protein Kinase ◽  
Leucine Rich Repeat

scholarly journals 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization

2010 ◽  
Vol 430 (3) ◽  
pp. 393-404 ◽  
Author(s):  
R. Jeremy Nichols ◽  
Nicolas Dzamko ◽  
Nicholas A. Morrice ◽  
David G. Campbell ◽  
Maria Deak ◽  
...  
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Protein Kinase ◽  
Inclusion Bodies ◽  
Kinase Activity ◽  
Protein Isoforms ◽  
Protein Kinase Activity ◽  
Leucine Rich Repeat ◽  
Pathogenic Mutations ◽  
Mouse Tissues

LRRK2 (leucine-rich repeat protein kinase 2) is mutated in a significant number of Parkinson's disease patients, but still little is understood about how it is regulated or functions. In the present study we have demonstrated that 14-3-3 protein isoforms interact with LRRK2. Consistent with this, endogenous LRRK2 isolated from Swiss 3T3 cells or various mouse tissues is associated with endogenous 14-3-3 isoforms. We have established that 14-3-3 binding is mediated by phosphorylation of LRRK2 at two conserved residues (Ser910 and Ser935) located before the leucine-rich repeat domain. Our results suggests that mutation of Ser910 and/or Ser935 to disrupt 14-3-3 binding does not affect intrinsic protein kinase activity, but induces LRRK2 to accumulate within discrete cytoplasmic pools, perhaps resembling inclusion bodies. To investigate links between 14-3-3 binding and Parkinson's disease, we studied how 41 reported mutations of LRRK2 affected 14-3-3 binding and cellular localization. Strikingly, we found that five of the six most common pathogenic mutations (R1441C, R1441G, R1441H, Y1699C and I2020T) display markedly reduced phosphorylation of Ser910/Ser935 thereby disrupting interaction with 14-3-3. We have also demonstrated that Ser910/Ser935 phosphorylation and 14-3-3 binding to endogenous LRRK2 is significantly reduced in tissues of homozygous LRRK2(R1441C) knock-in mice. Consistent with 14-3-3 regulating localization, all of the common pathogenic mutations displaying reduced 14-3-3-binding accumulated within inclusion bodies. We also found that three of the 41 LRRK2 mutations analysed displayed elevated protein kinase activity (R1728H, ~2-fold; G2019S, ~3-fold; and T2031S, ~4-fold). These results provide the first evidence suggesting that 14-3-3 regulates LRRK2 and that disruption of the interaction of LRRK2 with 14-3-3 may be linked to Parkinson's disease.

scholarly journals Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-like protein kinase genes in Arabidopsis thaliana

BMC Genomics ◽  
2010 ◽  
Vol 11 (1) ◽  
pp. 19 ◽  
Author(s):  
Xiaoping Gou ◽  
Kai He ◽  
Hui Yang ◽  
Tong Yuan ◽  
Honghui Lin ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Sequence Analysis ◽  
Protein Kinase ◽  
Leucine Rich Repeat ◽  
Genome Wide

scholarly journals Mechanistic analysis of the SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signaling

2018 ◽  
Author(s):  
Ulrich Hohmann ◽  
Joël Nicolet ◽  
Andrea Moretti ◽  
Ludwig A. Hothorn ◽  
Michael Hothorn
Keyword(s):  
Receptor Activation ◽  
Surface Patch ◽  
Receptor Kinase ◽  
Leucine Rich Repeat ◽  
Negative Regulators ◽  
Signaling Complex ◽  
The Core ◽  
Mechanistic Analysis ◽  
Brassinosteroid Signaling

AbstractThe leucine-rich repeat receptor kinase (LRR-RK) BRI1 requires a shape-complementary SERK co-receptor for brassinosteroid sensing and receptor activation. Interface mutations that weaken the interaction between receptor and co-receptor in vitro reduce brassinosteroid signaling responses. The SERK3 elongated (elg) allele maps to the complex interface and shows enhanced brassinosteroid signaling, but surprisingly no tighter binding to the BRI1 ectodomain in vitro. Here, we report that rather than promoting the interaction with BRI1, the elg mutation disrupts the ability of the co-receptor to interact with the ectodomains of BIR receptor pseudokinases, negative regulators of LRR-RK signaling. A conserved lateral surface patch in BIR LRR domains is required for targeting SERK co-receptors and the elg allele maps to the core of the complex interface in a 1.25 Å BIR3 - SERK1 structure. Collectively, our structural, quantitative biochemical and genetic analyses suggest that brassinosteroid signaling complex formation is negatively regulated by BIR receptor ectodomains.

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