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Article ; Online: The importance of cache domains in α

Page, Karen M / Gumerov, Vadim M / Dahimene, Shehrazade / Zhulin, Igor B / Dolphin, Annette C

2023 Volume 17, Issue 1, Page(s) 2167563

Abstract: In this hybrid review, we have first collected and reviewed available information on the structure and function of the enigmatic cache domains in ... ...

Abstract	In this hybrid review, we have first collected and reviewed available information on the structure and function of the enigmatic cache domains in α
MeSH term(s)	Calcium Channels/metabolism ; Gabapentin/metabolism ; Amines/metabolism ; Amines/pharmacology ; Cell Membrane/metabolism
Chemical Substances	Calcium Channels ; Gabapentin (6CW7F3G59X) ; Amines
Language	English
Publishing date	2023-02-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2262854-X
ISSN	1933-6969 ; 1933-6969
ISSN (online)	1933-6969
ISSN	1933-6969
DOI	10.1080/19336950.2023.2167563
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Article ; Online: The Interplay Between Splicing of Two Exon Combinations Differentially Affects Membrane Targeting and Function of Human Ca

Dahimene, Shehrazade / Page, Karen M / Nieto-Rostro, Manuela / Pratt, Wendy S / Dolphin, Annette C

Function (Oxford, England)

2023 Volume 5, Issue 1, Page(s) zqad060

Abstract: N-type calcium channels ( ... ...

Abstract	N-type calcium channels (Ca
MeSH term(s)	Humans ; Neurons/metabolism ; RNA Splicing ; Calcium Channels, N-Type/genetics ; Protein Isoforms/genetics ; Exons/genetics
Chemical Substances	Calcium Channels, N-Type ; Protein Isoforms
Language	English
Publishing date	2023-10-19
Publishing country	England
Document type	Journal Article
ISSN	2633-8823
ISSN (online)	2633-8823
DOI	10.1093/function/zqad060
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Article ; Online: ADAM17 Mediates Proteolytic Maturation of Voltage-Gated Calcium Channel Auxiliary α

Kadurin, Ivan / Dahimene, Shehrazade / Page, Karen M / Ellaway, Joseph I J / Chaggar, Kanchan / Troeberg, Linda / Nagase, Hideaki / Dolphin, Annette C

Function (Oxford, England)

2022 Volume 3, Issue 3, Page(s) zqac013

Abstract: The auxiliary ... ...

Abstract	The auxiliary α
MeSH term(s)	Humans ; Tissue Inhibitor of Metalloproteinase-3/metabolism ; Calcium Channels, N-Type/genetics ; Proteolysis ; Calcium, Dietary/metabolism ; Neuralgia ; Peptide Hydrolases/metabolism ; ADAM17 Protein/genetics
Chemical Substances	Tissue Inhibitor of Metalloproteinase-3 ; Calcium Channels, N-Type ; Calcium, Dietary ; Peptide Hydrolases (EC 3.4.-) ; ADAM17 protein, human (EC 3.4.24.86) ; ADAM17 Protein (EC 3.4.24.86)
Language	English
Publishing date	2022-03-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2633-8823
ISSN (online)	2633-8823
DOI	10.1093/function/zqac013
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Article ; Online: Biallelic CACNA2D1 loss-of-function variants cause early-onset developmental epileptic encephalopathy.

Dahimene, Shehrazade / von Elsner, Leonie / Holling, Tess / Mattas, Lauren S / Pickard, Jess / Lessel, Davor / Pilch, Kjara S / Kadurin, Ivan / Pratt, Wendy S / Zhulin, Igor B / Dai, Hongzheng / Hempel, Maja / Ruzhnikov, Maura R Z / Kutsche, Kerstin / Dolphin, Annette C

Brain : a journal of neurology

2022 Volume 145, Issue 8, Page(s) 2721–2729

Abstract: Voltage-gated calcium (CaV) channels form three subfamilies (CaV1-3). The CaV1 and CaV2 channels are heteromeric, consisting of an α1 pore-forming subunit, associated with auxiliary CaVβ and α2δ subunits. The α2δ subunits are encoded in mammals by four ... ...

Abstract	Voltage-gated calcium (CaV) channels form three subfamilies (CaV1-3). The CaV1 and CaV2 channels are heteromeric, consisting of an α1 pore-forming subunit, associated with auxiliary CaVβ and α2δ subunits. The α2δ subunits are encoded in mammals by four genes, CACNA2D1-4. They play important roles in trafficking and function of the CaV channel complexes. Here we report biallelic variants in CACNA2D1, encoding the α2δ-1 protein, in two unrelated individuals showing a developmental and epileptic encephalopathy. Patient 1 has a homozygous frameshift variant c.818_821dup/p.(Ser275Asnfs13) resulting in nonsense-mediated mRNA decay of the CACNA2D1 transcripts, and absence of α2δ-1 protein detected in patient-derived fibroblasts. Patient 2 is compound heterozygous for an early frameshift variant c.13_23dup/p.(Leu9Alafs5), highly probably representing a null allele and a missense variant c.626G>A/p.(Gly209Asp). Our functional studies show that this amino-acid change severely impairs the function of α2δ-1 as a calcium channel subunit, with strongly reduced trafficking of α2δ-1G209D to the cell surface and a complete inability of α2δ-1G209D to increase the trafficking and function of CaV2 channels. Thus, biallelic loss-of-function variants in CACNA2D1 underlie the severe neurodevelopmental disorder in these two patients. Our results demonstrate the critical importance and non-interchangeability of α2δ-1 and other α2δ proteins for normal human neuronal development.
MeSH term(s)	Age of Onset ; Animals ; Calcium ; Calcium Channels ; Calcium Channels, L-Type ; Calcium Channels, N-Type ; Cell Membrane ; Epilepsy ; Humans ; Mammals ; Neurons
Chemical Substances	CACNA2D1 protein, human ; Calcium Channels ; Calcium Channels, L-Type ; Calcium Channels, N-Type ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2022-03-11
Publishing country	England
Document type	Case Reports ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80072-7
ISSN	1460-2156 ; 0006-8950
ISSN (online)	1460-2156
ISSN	0006-8950
DOI	10.1093/brain/awac081
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Article ; Online: Disruption of the Key Ca

Meyer, James O / Dahimene, Shehrazade / Page, Karen M / Ferron, Laurent / Kadurin, Ivan / Ellaway, Joseph I J / Zhao, Pengxiang / Patel, Tarun / Rothwell, Simon W / Lin, Peipeng / Pratt, Wendy S / Dolphin, Annette C

Cell reports

2019 Volume 29, Issue 1, Page(s) 22–33.e5

Abstract: Voltage-gated calcium channels are exquisitely ... ...

Abstract	Voltage-gated calcium channels are exquisitely Ca
MeSH term(s)	Animals ; Binding Sites/physiology ; Calcium/metabolism ; Calcium Channels, N-Type/metabolism ; Cell Line ; Cell Membrane/metabolism ; Female ; Hippocampus/metabolism ; Humans ; Male ; Mice ; Neurites/metabolism ; Neurons/metabolism ; Protein Transport/physiology ; Rats ; Rats, Sprague-Dawley
Chemical Substances	Calcium Channels, N-Type ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2019-10-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2019.08.079
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Article ; Online: A CaV2.1 N-terminal fragment relieves the dominant-negative inhibition by an Episodic ataxia 2 mutant.

Dahimene, Shehrazade / Page, Karen M / Nieto-Rostro, Manuela / Pratt, Wendy S / D'Arco, Marianna / Dolphin, Annette C

Neurobiology of disease

2016 Volume 93, Page(s) 243–256

Abstract: Episodic ataxia 2 (EA2) is an autosomal dominant disorder caused by mutations in the gene CACNA1A that encodes the pore-forming CaV2.1 calcium channel subunit. The majority of EA2 mutations reported so far are nonsense or deletion/insertion mutations ... ...

Abstract	Episodic ataxia 2 (EA2) is an autosomal dominant disorder caused by mutations in the gene CACNA1A that encodes the pore-forming CaV2.1 calcium channel subunit. The majority of EA2 mutations reported so far are nonsense or deletion/insertion mutations predicted to form truncated proteins. Heterologous expression of wild-type CaV2.1, together with truncated constructs that mimic EA2 mutants, significantly suppressed wild-type calcium channel function, indicating that the truncated protein produces a dominant-negative effect (Jouvenceau et al., 2001; Page et al., 2004). A similar finding has been shown for CaV2.2 (Raghib et al., 2001). We show here that a highly conserved sequence in the cytoplasmic N-terminus is involved in this process, for both CaV2.1 and CaV2.2 channels. Additionally, we were able to interfere with the suppressive effect of an EA2 construct by mutating key N-terminal residues within it. We postulate that the N-terminus of the truncated channel plays an essential part in its interaction with the full-length CaV2.1, which prevents the correct folding of the wild-type channel. In agreement with this, we were able to disrupt the interaction between EA2 and the full length channel by co-expressing a free N-terminal peptide.
MeSH term(s)	Animals ; Ataxia/genetics ; Calcium Channels, N-Type/genetics ; Calcium Channels, N-Type/metabolism ; Cells, Cultured ; Membrane Potentials/drug effects ; Mutation/genetics ; Nystagmus, Pathologic/genetics ; Patch-Clamp Techniques/methods ; Rabbits ; Rats, Sprague-Dawley
Chemical Substances	Calcium Channels, N-Type ; voltage-dependent calcium channel (P-Q type)
Language	English
Publishing date	2016-05-31
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1211786-9
ISSN	1095-953X ; 0969-9961
ISSN (online)	1095-953X
ISSN	0969-9961
DOI	10.1016/j.nbd.2016.05.020
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Article ; Online: The α

Dahimene, Shehrazade / Page, Karen M / Kadurin, Ivan / Ferron, Laurent / Ho, Dominique Y / Powell, Gareth T / Pratt, Wendy S / Wilson, Stephen W / Dolphin, Annette C

Cell reports

2018 Volume 25, Issue 6, Page(s) 1610–1621.e5

Abstract: Voltage-gated calcium channel auxiliary α2δ subunits are important for channel trafficking and function. Here, we compare the effects of α2δ-1 and an α2δ-like protein called Cachd1 on neuronal N-type ( ... ...

Abstract	Voltage-gated calcium channel auxiliary α2δ subunits are important for channel trafficking and function. Here, we compare the effects of α2δ-1 and an α2δ-like protein called Cachd1 on neuronal N-type (Ca
MeSH term(s)	Animals ; Calcium Channels/genetics ; Calcium Channels/metabolism ; Calcium Channels, N-Type/genetics ; Calcium Channels, N-Type/metabolism ; Cell Membrane/metabolism ; Hippocampus/metabolism ; Ion Channel Gating ; Male ; Membrane Proteins/metabolism ; Mutation/genetics ; Neurites/metabolism ; Protein Binding ; Rats, Sprague-Dawley
Chemical Substances	Cachd1 protein, rat ; Calcium Channels ; Calcium Channels, N-Type ; Membrane Proteins
Language	English
Publishing date	2018-11-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2018.10.033
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Article ; Online: Genetic disruption of voltage-gated calcium channels in psychiatric and neurological disorders.

Heyes, Samuel / Pratt, Wendy S / Rees, Elliott / Dahimene, Shehrazade / Ferron, Laurent / Owen, Michael J / Dolphin, Annette C

Progress in neurobiology

2015 Volume 134, Page(s) 36–54

Abstract: This review summarises genetic studies in which calcium channel genes have been connected to the spectrum of neuropsychiatric syndromes, from bipolar disorder and schizophrenia to autism spectrum disorders and intellectual impairment. Among many other ... ...

Abstract	This review summarises genetic studies in which calcium channel genes have been connected to the spectrum of neuropsychiatric syndromes, from bipolar disorder and schizophrenia to autism spectrum disorders and intellectual impairment. Among many other genes, striking numbers of the calcium channel gene superfamily have been implicated in the aetiology of these diseases by various DNA analysis techniques. We will discuss how these relate to the known monogenic disorders associated with point mutations in calcium channels. We will then examine the functional evidence for a causative link between these mutations or single nucleotide polymorphisms and the disease processes. A major challenge for the future will be to translate the expanding psychiatric genetic findings into altered physiological function, involvement in the wider pathology of the diseases, and what potential that provides for personalised and stratified treatment options for patients.
MeSH term(s)	Animals ; Calcium Channels/genetics ; Calcium Channels/metabolism ; Humans ; Mental Disorders/drug therapy ; Mental Disorders/genetics ; Mental Disorders/metabolism ; Mutation ; Nervous System Diseases/drug therapy ; Nervous System Diseases/genetics ; Nervous System Diseases/metabolism ; Polymorphism, Single Nucleotide
Chemical Substances	Calcium Channels
Language	English
Publishing date	2015-09-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	185535-9
ISSN	1873-5118 ; 0301-0082
ISSN (online)	1873-5118
ISSN	0301-0082
DOI	10.1016/j.pneurobio.2015.09.002
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Article: LQT1-associated mutations increase KCNQ1 proteasomal degradation independently of Derlin-1.

Peroz, David / Dahimène, Shehrazade / Baró, Isabelle / Loussouarn, Gildas / Mérot, Jean

The Journal of biological chemistry

2008 Volume 284, Issue 8, Page(s) 5250–5256

Abstract: Mutations in the potassium channel KCNQ1 that determine retention of the mutated proteins in the endoplasmic reticulum (ER) are associated with the autosomal dominant negative Romano-Ward LQT1 cardiac syndrome. In the present study, we have analyzed the ... ...

Abstract	Mutations in the potassium channel KCNQ1 that determine retention of the mutated proteins in the endoplasmic reticulum (ER) are associated with the autosomal dominant negative Romano-Ward LQT1 cardiac syndrome. In the present study, we have analyzed the consequences and the potential molecular mechanisms involved in the ER retention of three Romano-Ward mutations located in KCNQ1 N terminus (Y111C, L114P, and P117L). We showed that the mutant KCNQ1 proteins exhibited reduced expression levels with respect to wild-type (WT)-KCNQ1. Radiolabeling pulse-chase experiments revealed that the lower expression levels did not result from reduced rate of synthesis. Instead, using a combination of Western blot and pulse-chase experiments, we showed that the mutant channel Y111C-KCNQ1, used as a model, was ubiquitinated and degraded in the proteasome more rapidly (t((1/2)) = 82 min) than WT-KCNQ1 channel (t((1/2)) = 113 min). On the other hand, KCNQ1 degradation did not appear to involve the GTP-dependent pathway. We also showed that KCNE1 stabilized both wild-type and Y111C proteins. To identify potential actors involved in KCNQ1 degradation, we studied the implication of the ER-resident protein Derlin-1 in KCNQ1 degradation. We showed that although KCNQ1 and Derlin-1 share the same molecular complex and co-immunoprecipitate when co-expressed in HEK293FT cells, Derlin-1 did not affect KCNQ1 steady state expression and degradation. These data were confirmed in T84 cells that express endogenous KCNQ1 and Derlin-1. Small interfering RNA knock-down of Derlin-1 did not modify KCNQ1 expression level, and no interaction between endogenous KCNQ1 and Derlin-1 could be detected.
MeSH term(s)	Amino Acid Substitution ; Cell Line ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Gene Expression Regulation/genetics ; Guanosine Triphosphate/metabolism ; Humans ; KCNQ1 Potassium Channel/genetics ; KCNQ1 Potassium Channel/metabolism ; Membrane Proteins/antagonists & inhibitors ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mutation, Missense ; Proteasome Endopeptidase Complex/genetics ; Proteasome Endopeptidase Complex/metabolism ; RNA, Small Interfering ; Romano-Ward Syndrome/genetics ; Romano-Ward Syndrome/metabolism ; Ubiquitination/genetics
Chemical Substances	DERL1 protein, human ; KCNQ1 Potassium Channel ; KCNQ1 protein, human ; Membrane Proteins ; RNA, Small Interfering ; Guanosine Triphosphate (86-01-1) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2008-12-29
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M806459200
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Article: LQT1-associated Mutations Increase KCNQ1 Proteasomal Degradation Independently of Derlin-1

Peroz, David / Dahimène, Shehrazade / Baró, Isabelle / Loussouarn, Gildas / Mérot, Jean

Journal of biological chemistry. 2009 Feb. 20, v. 284, no. 8

2009

Abstract	Mutations in the potassium channel KCNQ1 that determine retention of the mutated proteins in the endoplasmic reticulum (ER) are associated with the autosomal dominant negative Romano-Ward LQT1 cardiac syndrome. In the present study, we have analyzed the consequences and the potential molecular mechanisms involved in the ER retention of three Romano-Ward mutations located in KCNQ1 N terminus (Y111C, L114P, and P117L). We showed that the mutant KCNQ1 proteins exhibited reduced expression levels with respect to wild-type (WT)-KCNQ1. Radiolabeling pulse-chase experiments revealed that the lower expression levels did not result from reduced rate of synthesis. Instead, using a combination of Western blot and pulse-chase experiments, we showed that the mutant channel Y111C-KCNQ1, used as a model, was ubiquitinated and degraded in the proteasome more rapidly (t[fraction one₋half] = 82 min) than WT-KCNQ1 channel (t[fraction one₋half] = 113 min). On the other hand, KCNQ1 degradation did not appear to involve the GTP-dependent pathway. We also showed that KCNE1 stabilized both wild-type and Y111C proteins. To identify potential actors involved in KCNQ1 degradation, we studied the implication of the ER-resident protein Derlin-1 in KCNQ1 degradation. We showed that although KCNQ1 and Derlin-1 share the same molecular complex and co-immunoprecipitate when co-expressed in HEK293FT cells, Derlin-1 did not affect KCNQ1 steady state expression and degradation. These data were confirmed in T84 cells that express endogenous KCNQ1 and Derlin-1. Small interfering RNA knock-down of Derlin-1 did not modify KCNQ1 expression level, and no interaction between endogenous KCNQ1 and Derlin-1 could be detected.
Language	English
Dates of publication	2009-0220
Size	p. 5250-5256.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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