Faculty Opinions recommendation of Roles for rice membrane dynamics and plasmodesmata during biotrophic invasion by the blast fungus.

Our laboratory is concerned with understanding the dynamic structure of the plasma membrane with particular reference to the movement of membrane constituents during cell locomotion. In addition to the standard tools of molecular cell biology, we employ both fluorescence recovery after photo- bleaching (FRAP) and digitized fluorescence microscopy (DFM) to investigate individual cells. FRAP allows the measurement of translational mobility of membrane and cytoplasmic molecules in small regions of single, living cells. DFM is really a new form of light microscopy in that the distribution of individual classes of ions, molecules, and macromolecules can be followed in single, living cells. By employing fluorescent antibodies to defined antigens or fluorescent analogs of cellular constituents as well as ultrasensitive, electronic image detectors and video image averaging to improve signal to noise, fluorescent images of living cells can be acquired over an extended period without significant fading and loss of cell viability.

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Coaction of Electrostatic and Hydrophobic Interactions: Dynamic Constraints on Disordered TrkA Juxtamembrane Domain

10.26434/chemrxiv.9847190 ◽

2019 ◽

Author(s):

Zichen Wang ◽

Huaxun Fan ◽

Xiao Hu ◽

John Khamo ◽

Jiajie Diao ◽

...

Keyword(s):

Single Molecule ◽

Protein Function ◽

Hydrophobic Interactions ◽

Transmembrane Helix ◽

Point Mutations ◽

Salt Bridge ◽

Receptor Activation ◽

Membrane Dynamics ◽

Juxtamembrane Domain ◽

Joint Work

<p>The receptor tyrosine kinase family transmits signals into cell via a single transmembrane helix and a flexible juxtamembrane domain (JMD). Membrane dynamics makes it challenging to study the structural mechanism of receptor activation experimentally. In this study, we employ all-atom molecular dynamics with Highly Mobile Membrane-Mimetic to capture membrane interactions with the JMD of tropomyosin receptor kinase A (TrkA). We find that PIP<sub>2 </sub>lipids engage in lasting binding to multiple basic residues and compete with salt bridge within the peptide. We discover three residues insertion into the membrane, and perturb it through computationally designed point mutations. Single-molecule experiments indicate the contribution from hydrophobic insertion is comparable to electrostatic binding, and in-cell experiments show that enhanced TrkA-JMD insertion promotes receptor ubiquitination. Our joint work points to a scenario where basic and hydrophobic residues on disordered domains interact with lipid headgroups and tails, respectively, to restrain flexibility and potentially modulate protein function.</p>

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Faculty Opinions recommendation of Regulation of maternal phospholipid composition and IP(3)-dependent embryonic membrane dynamics by a specific fatty acid metabolic event in C. elegans.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.14264040.789502810 ◽

2012 ◽

Author(s):

Wendy Hanna-Rose ◽

Tracy Vrablik

Keyword(s):

Fatty Acid ◽

Phospholipid Composition ◽

Membrane Dynamics ◽

Specific Fatty Acid ◽

C Elegans ◽

Metabolic Event

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Analyzing Avirulence Genes of Magnaporthe oryzae from Heilongjiang Pro- vince and Screening Rice Germplasm with Resistance to Blast Fungus

ACTA AGRONOMICA SINICA ◽

10.3724/sp.j.1006.2012.02192 ◽

2013 ◽

Vol 38 (12) ◽

pp. 2192-2197 ◽

Cited By ~ 4

Author(s):

Xiang-Xiao LI ◽

Qian WANG ◽

Sheng-Xiang LUO ◽

Yun-Xia HE ◽

Ling-Hua ZHU ◽

...

Keyword(s):

Magnaporthe Oryzae ◽

Avirulence Genes ◽

Rice Germplasm ◽

Blast Fungus

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Structural catalog of core Atg proteins opens new era of autophagy research

The Journal of Biochemistry ◽

10.1093/jb/mvab017 ◽

2021 ◽

Author(s):

Kazuaki Matoba ◽

Nobuo N Noda

Keyword(s):

De Novo ◽

Structural Information ◽

Membrane Dynamics ◽

Autophagosome Formation ◽

New Era ◽

Intracellular Degradation ◽

Atg Proteins ◽

Biological Studies ◽

Evolutionarily Conserved ◽

Biological Methods

Summary Autophagy, which is an evolutionarily conserved intracellular degradation system, involves de novo generation of autophagosomes that sequester and deliver diverse cytoplasmic materials to the lysosome for degradation. Autophagosome formation is mediated by approximately 20 core autophagy-related (Atg) proteins, which collaborate to mediate complicated membrane dynamics during autophagy. To elucidate the molecular functions of these Atg proteins in autophagosome formation, many researchers have tried to determine the structures of Atg proteins by using various structural biological methods. Although not sufficient, the basic structural catalog of all core Atg proteins was established. In this review article, we summarize structural biological studies of core Atg proteins, with an emphasis on recently unveiled structures, and describe the mechanistic breakthroughs in autophagy research that have derived from new structural information.

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