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Article ; Online: Lysosomal channels sensing forces.

Riederer, Erika / Ren, Dejian

2024 Volume 26, Issue 3, Page(s) 318–320

MeSH term(s)	Lysosomes
Language	English
Publishing date	2024-02-22
Publishing country	England
Document type	Journal Article
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/s41556-024-01347-5
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Article ; Online: Lysosomal Ion Channels: What Are They Good For and Are They Druggable Targets?

Riederer, Erika / Cang, Chunlei / Ren, Dejian

Annual review of pharmacology and toxicology

2022 Volume 63, Page(s) 19–41

Abstract: Lysosomes play fundamental roles in material digestion, cellular clearance, recycling, exocytosis, wound repair, ... ...

Abstract	Lysosomes play fundamental roles in material digestion, cellular clearance, recycling, exocytosis, wound repair, Ca
MeSH term(s)	Humans ; Ion Channels/metabolism ; Signal Transduction ; Lysosomes/chemistry ; Lysosomes/metabolism ; Neurodegenerative Diseases/metabolism
Chemical Substances	Ion Channels
Language	English
Publishing date	2022-09-23
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	196587-6
ISSN	1545-4304 ; 0362-1642
ISSN (online)	1545-4304
ISSN	0362-1642
DOI	10.1146/annurev-pharmtox-051921-013755
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Book: Regulation of lysosomal function by organelle sodium and potassium channels

Ren, Dejian

(NIH neuroscience seminar)

2015

Abstract: CIT): Cellular excitability influences essentially every aspect of life, from fertilization to breathing and heart beating. The major interests of Dr. Ren"s lab concern the regulation of cellular excitability, neuronal network activity and animal ... ...

Institution	National Institutes of Health (U.S.),
Author's details	Dejian Ren
Series title	NIH neuroscience seminar
Abstract	(CIT): Cellular excitability influences essentially every aspect of life, from fertilization to breathing and heart beating. The major interests of Dr. Ren"s lab concern the regulation of cellular excitability, neuronal network activity and animal behavior by ion channels, G-protein coupled receptors, tyrosine kinases and calcium signaling. A recent focus in the lab is to study the molecular mechanisms of neuronal excitability control by extracelular ions and peptide neurotransmitters. Significant changes in extracellular Ca2+ concentrations ([Ca2+]e) can happen in certain brain areas during physiological and pathological conditions such as seizures and brain ischemia. They are interested in understanding at the molecular level how neurons sense the [Ca2+]e changes, how the information is transmitted to the intracellular second messenger system, and how neuronal circuit function is affected by the signaling. Numerous neuropeptides are used by the nervous systems as chemical signals to regulate physiological processes such as feeding, rewarding, pain sensation, arousal and wakefulness. They are interested in how several neuropeptides influence the electrical properties of individual neurons in various brain regions and spinal cord. Along this line, they discovered a novel ion channel activation mechanism by G-protein coupled receptors: it is independent of G-protein activation but requires the Src family of tyrosine kinases and two largely uncharacterized proteins UNC79 and UNC80. Current efforts in this project focus on uncovering how the receptor activation is coupled to channel opening and how such signaling events contribute to the intrinsic properties of neurons under physiological and pathophysiological conditions. Another area of research in the lab concerns rhythm generation. All animals display long-period rhythmic behaviors such as circadian rhythm (~ 24 hours), as well as ones with shorter periods such as locomotion, heart beating, and breathing (milliseconds to seconds). They are interested in the molecular mechanisms underlying the generation and modulation of the "short-period" rhythms. They use an integrative approach to study the physiological problems. At the molecular level, they use molecular biology and protein chemistry to study channel proteins and their associated partners. They use electrophysiology methods to record the electrical activities from a single molecule (single channel recording), a whole cell, or a nerve bundle. At the cellular level, they use high-speed fluorescence confocal microscopy to image dynamics of ions and protein molecules inside the cells. At the systems level, they modify the genomes of animals and study the consequences of such modifications on whole organism physiology and behavior.
MeSH term(s)	Lysosomes/physiology ; Sodium Channels ; Potassium Channels ; Sodium-Potassium-Exchanging ATPase/physiology
Language	English
Size	1 online resource (1 streaming video file (59 min.)) :, color, sound.
Document type	Book
Note	Closed-captioned.
Database	Catalogue of the US National Library of Medicine (NLM)

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Article ; Online: Two-pore channels regulate endomembrane tension to enable remodeling and resolution of phagolysosomes.

Chadwick, Sarah R / Barreda, Dante / Wu, Jing Ze / Ye, Gang / Yusuf, Bushra / Ren, Dejian / Freeman, Spencer A

Proceedings of the National Academy of Sciences of the United States of America

2024 Volume 121, Issue 8, Page(s) e2309465121

Abstract: Phagocytes promptly resolve ingested targets to replenish lysosomes and maintain their responsiveness. The resolution process requires that degradative hydrolases, solute transporters, and proteins involved in lipid traffic are delivered and made active ... ...

Abstract	Phagocytes promptly resolve ingested targets to replenish lysosomes and maintain their responsiveness. The resolution process requires that degradative hydrolases, solute transporters, and proteins involved in lipid traffic are delivered and made active in phagolysosomes. It also involves extensive membrane remodeling. We report that cation channels that localize to phagolysosomes were essential for resolution. Specifically, the conductance of Na
MeSH term(s)	Mice ; Animals ; Two-Pore Channels ; Phagosomes/metabolism ; Lysosomes/metabolism ; Hydrolases/metabolism ; Cholesterol/metabolism
Chemical Substances	Two-Pore Channels ; Hydrolases (EC 3.-) ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2024-02-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2309465121
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Article ; Online: Calcium signaling in sperm: help from prostasomes.

Ren, Dejian

Science signaling

2011 Volume 4, Issue 173, Page(s) pe27

Abstract: Mammalian sperm cells are equipped with sophisticated Ca2+ signaling mechanisms that are fundamental to sperm's success in fertilization. Unlike most other cells, however, mature sperm generally do not have the luxury of synthesizing new proteins. New ... ...

Abstract	Mammalian sperm cells are equipped with sophisticated Ca2+ signaling mechanisms that are fundamental to sperm's success in fertilization. Unlike most other cells, however, mature sperm generally do not have the luxury of synthesizing new proteins. New evidence indicates that human sperm have a very clever way to solve the conflict between the critical demand for Ca2+ signaling tools and the silence of protein translation. Just before encountering the female reproductive tract, sperm acquire some of the key molecules for Ca2+ signaling from the male reproductive tract itself: prostasomes secreted by the prostate gland.
MeSH term(s)	Calcium Signaling ; Female ; Humans ; Male ; Prostate/secretion ; Spermatozoa/metabolism
Language	English
Publishing date	2011-05-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2417226-1
ISSN	1937-9145 ; 1945-0877
ISSN (online)	1937-9145
ISSN	1945-0877
DOI	10.1126/scisignal.2002102
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Article ; Online: Sodium leak channels in neuronal excitability and rhythmic behaviors.

Ren, Dejian

Neuron

2011 Volume 72, Issue 6, Page(s) 899–911

Abstract: Extracellular K⁺, Na⁺, and Ca²⁺ ions all influence the resting membrane potential of the neuron. However, the mechanisms by which extracellular Na⁺ and Ca²⁺ regulate basal neuronal excitability are not well understood. Recent findings suggest that NALCN, ...

Abstract	Extracellular K⁺, Na⁺, and Ca²⁺ ions all influence the resting membrane potential of the neuron. However, the mechanisms by which extracellular Na⁺ and Ca²⁺ regulate basal neuronal excitability are not well understood. Recent findings suggest that NALCN, in association with UNC79 and UNC80, contributes a basal Na⁺ leak conductance in neurons. Mutations in Nalcn, Unc79, or Unc80 lead to severe phenotypes that include neonatal lethality and disruption in rhythmic behaviors. This review discusses the properties of the NALCN complex, its regulation, and its contribution to neuronal function and animal behavior.
MeSH term(s)	Amino Acid Sequence ; Animals ; Humans ; Ion Channels ; Membrane Proteins ; Molecular Sequence Data ; Neurons/physiology ; Periodicity ; Potassium Channels, Tandem Pore Domain/chemistry ; Potassium Channels, Tandem Pore Domain/physiology ; Sodium Channels/chemistry ; Sodium Channels/physiology
Chemical Substances	Ion Channels ; Membrane Proteins ; NALCN protein, human ; Potassium Channels, Tandem Pore Domain ; Sodium Channels
Language	English
Publishing date	2011-12-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	808167-0
ISSN	1097-4199 ; 0896-6273
ISSN (online)	1097-4199
ISSN	0896-6273
DOI	10.1016/j.neuron.2011.12.007
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Zs.MG 92: Show issues

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Article ; Online: Sperm and the proton channel.

Ren, Dejian

The New England journal of medicine

2010 Volume 362, Issue 20, Page(s) 1934–1935

MeSH term(s)	Acrosome Reaction ; Calcium Channels/metabolism ; Humans ; Hydrogen-Ion Concentration ; Ion Channels/metabolism ; Male ; Patch-Clamp Techniques ; Sperm Capacitation/physiology ; Spermatozoa/metabolism
Chemical Substances	Calcium Channels ; HVCN1 protein, human ; Ion Channels
Language	English
Publishing date	2010-02-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	207154-x
ISSN	1533-4406 ; 0028-4793
ISSN (online)	1533-4406
ISSN	0028-4793
DOI	10.1056/NEJMcibr1001843
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Article ; Online: NALCN channels enhance the intrinsic excitability of spinal projection neurons.

Ford, Neil C / Ren, Dejian / Baccei, Mark L

Pain

2018 Volume 159, Issue 9, Page(s) 1719–1730

Abstract: Spinal projection neurons convey nociceptive signals to multiple brain regions including the parabrachial (PB) nucleus, which contributes to the emotional valence of pain perception. Despite the clear importance of projection neurons to pain processing, ... ...

Abstract	Spinal projection neurons convey nociceptive signals to multiple brain regions including the parabrachial (PB) nucleus, which contributes to the emotional valence of pain perception. Despite the clear importance of projection neurons to pain processing, our understanding of the factors that shape their intrinsic membrane excitability remains limited. Here, we investigate a potential role for the Na leak channel NALCN in regulating the activity of spino-PB neurons in the developing rodent. Pharmacological reduction of NALCN current (INALCN), or the genetic deletion of NALCN channels, significantly reduced the intrinsic excitability of lamina I spino-PB neurons. In addition, substance P (SP) activated INALCN in ascending projection neurons through downstream Src kinase signaling, and the knockout of NALCN prevented SP-evoked action potential discharge in this neuronal population. These results identify, for the first time, NALCN as a strong regulator of neuronal activity within central pain circuits and also elucidate an additional ionic mechanism by which SP can modulate spinal nociceptive processing. Collectively, these findings indicate that the level of NALCN conductance within spino-PB neurons tightly governs ascending nociceptive transmission to the brain and thereby potentially influences pain perception.
MeSH term(s)	Action Potentials/physiology ; Animals ; Animals, Newborn ; Ion Channels/genetics ; Ion Channels/metabolism ; Membrane Proteins ; Mice ; Mice, Knockout ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Parabrachial Nucleus/cytology ; Parabrachial Nucleus/metabolism ; Posterior Horn Cells/cytology ; Posterior Horn Cells/metabolism ; Rats ; Rats, Sprague-Dawley ; Spinal Cord/cytology ; Spinal Cord/metabolism
Chemical Substances	Ion Channels ; Membrane Proteins ; NALCN protein, mouse ; Nerve Tissue Proteins
Language	English
Publishing date	2018-05-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	193153-2
ISSN	1872-6623 ; 0304-3959
ISSN (online)	1872-6623
ISSN	0304-3959
DOI	10.1097/j.pain.0000000000001258
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Article ; Online: Lysosomal physiology.

Xu, Haoxing / Ren, Dejian

Annual review of physiology

2015 Volume 77, Page(s) 57–80

Abstract: Lysosomes are acidic compartments filled with more than 60 different types of hydrolases. They mediate the degradation of extracellular particles from endocytosis and of intracellular components from autophagy. The digested products are transported out ... ...

Abstract	Lysosomes are acidic compartments filled with more than 60 different types of hydrolases. They mediate the degradation of extracellular particles from endocytosis and of intracellular components from autophagy. The digested products are transported out of the lysosome via specific catabolite exporters or via vesicular membrane trafficking. Lysosomes also contain more than 50 membrane proteins and are equipped with the machinery to sense nutrient availability, which determines the distribution, number, size, and activity of lysosomes to control the specificity of cargo flux and timing (the initiation and termination) of degradation. Defects in degradation, export, or trafficking result in lysosomal dysfunction and lysosomal storage diseases (LSDs). Lysosomal channels and transporters mediate ion flux across perimeter membranes to regulate lysosomal ion homeostasis, membrane potential, catabolite export, membrane trafficking, and nutrient sensing. Dysregulation of lysosomal channels underlies the pathogenesis of many LSDs and possibly that of metabolic and common neurodegenerative diseases.
MeSH term(s)	Animals ; Exocytosis/physiology ; Homeostasis/physiology ; Humans ; Ion Channels/physiology ; Ions/metabolism ; Lysosomal Storage Diseases/physiopathology ; Lysosomes/physiology ; Membrane Potentials/physiology
Chemical Substances	Ion Channels ; Ions
Language	English
Publishing date	2015
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	207933-1
ISSN	1545-1585 ; 0066-4278
ISSN (online)	1545-1585
ISSN	0066-4278
DOI	10.1146/annurev-physiol-021014-071649
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Article ; Online: A new neurodevelopmental disorder linked to heterozygous variants in UNC79.

Bayat, Allan / Liu, Zhenjiang / Luo, Sheng / Fenger, Christina D / Højte, Anne F / Isidor, Bertrand / Cogne, Benjamin / Larson, Austin / Zanus, Caterina / Faletra, Flavio / Keren, Boris / Musante, Luciana / Gourfinkel-An, Isabelle / Perrine, Charles / Demily, Caroline / Lesca, Gaeton / Liao, Weiping / Ren, Dejian

Genetics in medicine : official journal of the American College of Medical Genetics

2023 Volume 25, Issue 9, Page(s) 100894

Abstract: Purpose: The "NALCN channelosome" is an ion channel complex that consists of multiple proteins, including NALCN, UNC79, UNC80, and FAM155A. Only a small number of individuals with a neurodevelopmental syndrome have been reported with disease causing ... ...

Abstract	Purpose: The "NALCN channelosome" is an ion channel complex that consists of multiple proteins, including NALCN, UNC79, UNC80, and FAM155A. Only a small number of individuals with a neurodevelopmental syndrome have been reported with disease causing variants in NALCN and UNC80. However, no pathogenic UNC79 variants have been reported, and in vivo function of UNC79 in humans is largely unknown. Methods: We used international gene-matching efforts to identify patients harboring ultrarare heterozygous loss-of-function UNC79 variants and no other putative responsible genes. We used genetic manipulations in Drosophila and mice to test potential causal relationships between UNC79 variants and the pathology. Results: We found 6 unrelated and affected patients with UNC79 variants. Five patients presented with overlapping neurodevelopmental features, including mild to moderate intellectual disability and a mild developmental delay, whereas a single patient reportedly had normal cognitive and motor development but was diagnosed with epilepsy and autistic features. All displayed behavioral issues and 4 patients had epilepsy. Drosophila with UNC79 knocked down displayed induced seizure-like phenotype. Mice with a heterozygous loss-of-function variant have a developmental delay in body weight compared with wild type. In addition, they have impaired ability in learning and memory. Conclusion: Our results demonstrate that heterozygous loss-of-function UNC79 variants are associated with neurologic pathologies.
MeSH term(s)	Animals ; Humans ; Mice ; Drosophila/genetics ; Epilepsy ; Intellectual Disability/genetics ; Intellectual Disability/pathology ; Neurodevelopmental Disorders/genetics ; Phenotype ; Membrane Proteins/genetics
Chemical Substances	Membrane Proteins
Language	English
Publishing date	2023-05-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1455352-1
ISSN	1530-0366 ; 1098-3600
ISSN (online)	1530-0366
ISSN	1098-3600
DOI	10.1016/j.gim.2023.100894
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