Jasmonate perception by inositol phosphate-potentiated COI1-JAZ co-receptor
- Laura B. Sheard, Xu Tan, N. Zheng
- BiologyNature
- 24 August 2010
The mechanism of jasmonate perception is unraveled, the ability of F-box proteins to evolve as multi-component signalling hubs is highlighted and inositol pentakisphosphate is identified, which interacts with both COI1 and JAZ adjacent to the ligand.
The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20.
- Xuelian Luo, Zhanyun Tang, J. Rizo, Hongtao Yu
- BiologyMolecules and Cells
- 2002
A conformational switch in syntaxin during exocytosis: role of munc18
- I. Dulubova, S. Sugita, J. Rizo
- Biology, ChemistryEMBO Journal
- 16 August 1999
The results indicate that syntaxin binds to munc18‐1 in a closed conformation and suggest that this conformation represents an essential intermediate in exocytosis, and suggest a model whereby syntaxin undergoes a large conformational switch that mediates the transition between the syntaxin–munc 18‐1 complex and the core complex.
Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3.
- Huayi Wang, Liming Sun, Xiaodong Wang
- BiologyMolecules and Cells
- 10 April 2014
The Mad2 spindle checkpoint protein has two distinct natively folded states
- Xuelian Luo, Zhanyun Tang, Hongtao Yu
- Biology, ChemistryNature Structural &Molecular Biology
- 14 March 2004
It is shown that without cofactor binding or covalent modification Mad2 adopts two distinct folded conformations at equilibrium (termed N1-Mad2 and N2-Mad1), suggesting that the unusual two-state behavior of Mad2 is critical for spindle checkpoint signaling.
Snares and munc18 in synaptic vesicle fusion
An increasing amount of information derived from a convergence of structural, physiological and genetic studies is providing important insights into the mechanism of neurotransmitter release.
Reconstitution of the Vital Functions of Munc18 and Munc13 in Neurotransmitter Release
- Cong Ma, L. Su, A. B. Seven, Yibin Xu, J. Rizo
- BiologyScience
- 25 January 2013
A model of neurotransmitter release explains why two proteins not needed for membrane fusion in vitro are needed in vivo and proposes that fusion does not proceed through syntaxin–SNAP-25 heterodimers but starts with the syntaxin-1–Munc18-1 complex.
The membrane fusion enigma: SNAREs, Sec1/Munc18 proteins, and their accomplices--guilty as charged?
Neurotransmitter release is governed by proteins that have homo-logs in most types of intracellular membrane fusion, including the Sec1/Munc18 protein Munc18-1 and the SNARE proteins syntaxin-1,…
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