Correction

Lysophosphatidic acid directly activates TRPV1 through a C-terminal binding site (vol 8, pg 78, 2012)

期刊

NATURE CHEMICAL BIOLOGY
卷 8, 期 8, 页码 737-737

出版社

NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio0812-737c

关键词

-

向作者/读者索取更多资源

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

推荐

Article Anatomy & Morphology

Chordacentrum mineralization is delayed in zebrafish betaglycan-null mutants

Tonatiuh Molina-Villa, Lizbeth Ramirez-Vidal, Valentin Mendoza, Diana Escalante-Alcalde, Fernando Lopez-Casillas

Summary: In this study, zebrafish Tgfbr3-null mutants were generated using CRISPR/Cas9 technology. The mutants showed unaltered embryonic angiogenesis and developed into fertile adults. A consistent phenotype in these mutants was delayed chordacentra mineralization, which did not lead to vertebral abnormalities in adult fishes.

DEVELOPMENTAL DYNAMICS (2022)

Article Biology

Discovery and characterization of Hv1-type proton channels in reef-building corals

Gisela Rangel-Yescas, Cecilia Cervantes, Miguel A. Cervantes-Rocha, Esteban Suarez-Delgado, Anastazia T. Banaszak, Ernesto Maldonado, Ian Scott Ramsey, Tamara Rosenbaum, Leon D. Islas

Summary: The study identified the presence of genes encoding voltage-dependent proton channels in reef-building corals and characterized their biophysical properties. An allosteric gating model was developed to provide mechanistic insight into the modulation of voltage-dependence by protons.
Editorial Material Neurosciences

Closing in on the heat-activation mechanisms of TRV channels

Leon D. Islas

JOURNAL OF PHYSIOLOGY-LONDON (2021)

Review Neurosciences

TRP channels: a journey towards a molecular understanding of pain

Tamara Rosenbaum, Sara L. Morales-Lazaro, Leon D. Islas

Summary: Recent studies on transient receptor potential (TRP) channel structure have provided valuable insights into their role in normal sensations and pain. This review article examines the recent advances in understanding the relationship between the structure and function of TRP ion channels and their involvement in pain. The perception of nociceptive signals and the avoidance of pain are crucial for survival. TRP channels, as transducers of harmful signals, play a significant role in detecting and translating these signals into pain. Cryogenic electron microscopy has allowed researchers to explore the molecular details of TRP channels, complementing functional studies and enhancing our understanding of their contribution to pain generation and maintenance.

NATURE REVIEWS NEUROSCIENCE (2022)

Article Neurosciences

Modes of action of lysophospholipids as endogenous activators of the TRPV4 ion channel

Miguel Benitez-Angeles, Ana E. Lopez Romero, Itzel Llorente, Ileana Hernandez-Araiza, Ariela Vergara-Jaque, Fernando H. Real, Oscar Eduardo Gutierrez Castaneda, Marcelino Arciniega, Luis E. Morales-Buenrostro, Francisco Torres-Quiroz, Refugio Garcia-Villegas, Luis B. Tovar-y-Romo, Wolfgang B. Liedtke, Leon D. Islas, Tamara Rosenbaum

Summary: In this study, it was found that the TRPV4 channel is activated by lysophosphatidic acid (LPA), making it one of the few known endogenous agonists for TRPV4. Mechanistic details of the activation of TRPV4 by LPA and lysophosphatidylcholine (LPC) were also provided, demonstrating that LPA interacts with both the N- and C-terminal regions of TRPV4 to activate this channel. Furthermore, it was shown that LPC activates TRPV4 by producing an open state with a different conductance than LPA.

JOURNAL OF PHYSIOLOGY-LONDON (2023)

Article Biochemical Research Methods

How to study a highly toxic protein to bacteria: A case of voltage sensor domain of mouse sperm-specific sodium/proton exchanger

Cesar Arcos-Hernandez, Esteban Suarez-Delgado, Leon D. Islas, Francisco Romero, Ignacio Lopez-Gonzalez, Hui-Wang Ai, Takuya Nishigaki

Summary: Heterologous expression systems are important for studying protein function, but some proteins can be toxic to bacteria, hindering vector preparation. In this study, we overcame this problem by inserting amber stop codons or synthetic introns, allowing successful expression of the protein of interest in HEK293 cells.

PROTEIN EXPRESSION AND PURIFICATION (2023)

Article Biology

Activation-pathway transitions in human voltage-gated proton channels revealed by a non-canonical fluorescent amino acid

Esteban Suarez-Delgado, Maru Orozco-Contreras, Gisela E. Rangel-Yescas, Leon D. Islas

Summary: Through patch-clamp fluorometry combined with the incorporation of fluorescent non-canonical amino acid Anap, we have obtained data on the voltage-dependent opening mechanism of H(V)1 channels. Our results suggest that motion of the S4 helix relative to an aromatic residue in the S2 helix leads to fluorescence increases upon depolarization, and Anap is quenched by this residue. Additionally, we found that the absolute value of the pH can impact the movement of the voltage sensor after channel opening.
Article Biology

Plpp3, a novel regulator of pluripotency exit and endodermal differentiation of mouse embryonic stem cells

Martha E. Montane-Romero, Ana V. Martinez-Silva, Augusto C. Poot-Hernandez, Diana Escalante-Alcalde

Summary: In recent decades, the study of bioactive lipids such as LPA and S1P has increased due to their involvement in regulating various processes. PLPP3 has been identified as a key player in maintaining the balance of these lipids and their signaling, and it may also play a role in endoderm development. This study used mouse ESCs to investigate the function of PLPP3 in self-renewal and differentiation, and found that PLPP3 deficiency primarily affected endoderm formation. Impaired endoderm differentiation was associated with decreased YAP1 nuclear localization, and these phenotypes were rescued by restoring the expression of catalytically active hPLPP3.

BIOLOGY OPEN (2023)

Article Biology

Unconventional interactions of the TRPV4 ion channel with beta-adrenergic receptor ligands

Miguel Benitez-Angeles, Emmanuel Juarez-Gonzalez, Ariela Vergara-Jaque, Itzel Llorente, Gisela Rangel-Yescas, Stephanie C. Thebault, Marcia Hiriart, Leon D. Islas, Tamara Rosenbaum

Summary: The TRPV4 ion channel, present in various tissues, has been associated with diseases such as skeletal dysplasias, neuromuscular disorders, and respiratory malfunction. This study reveals that the bronchodilator salbutamol can inhibit TRPV4's activation by interacting with specific residues and causing channel closing through an allosteric mechanism.

LIFE SCIENCE ALLIANCE (2022)

Review Physiology

Molecular Physiology of TRPV Channels: Controversies and Future Challenges

Tamara Rosenbaum, Leon D. Islas

Summary: The ability to detect environmental stimuli is crucial for survival, and ion channels, such as TRP proteins, play a key role in this process. The TRPV subfamily, which belongs to the TRP family, responds to various chemical and physical changes. Despite intensive research in the past two decades, controversies still exist regarding the function of these proteins due to their complexity. In this article, we discuss important features of their regulation and highlight efforts to advance the field.

ANNUAL REVIEW OF PHYSIOLOGY (2023)

Article Physiology

Permeant cations modulate pore dynamics and gating of TRPV1 ion channels

Miriam Garcia-Avila, Javier Tello-Marmolejo, Tamara Rosenbaum, Leon D. Islas

Summary: TRPV1 ion channels play important roles in thermal and chemical sensation, as well as in pathological states. This study reveals that large cations are more permeable than smaller ones and uncovers fast conformational changes modulated by the cation occupying the pore. The findings also demonstrate that ion permeation influences the voltage dependence of TRPV1 channels.

JOURNAL OF GENERAL PHYSIOLOGY (2023)

暂无数据