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Article ; Online: Missense variants in phospholamban and cardiac myosin binding protein identified in patients with a family history and clinical diagnosis of dilated cardiomyopathy.

Armanious, Gareth P / Lemieux, M Joanne / Espinoza-Fonseca, L Michel / Young, Howard S

Biochimica et biophysica acta. Molecular cell research

2024 Volume 1871, Issue 4, Page(s) 119699

Abstract: As the genetic landscape of cardiomyopathies continues to expand, the identification of missense variants in disease-associated genes frequently leads to a classification of variant of uncertain significance (VUS). For the proper reclassification of such ...

Abstract	As the genetic landscape of cardiomyopathies continues to expand, the identification of missense variants in disease-associated genes frequently leads to a classification of variant of uncertain significance (VUS). For the proper reclassification of such variants, functional characterization is an important contributor to the proper assessment of pathogenic potential. Several missense variants in the calcium transport regulatory protein phospholamban have been associated with dilated cardiomyopathy. However, >40 missense variants in this transmembrane peptide are currently known and most remain classified as VUS with little clinical information. Similarly, missense variants in cardiac myosin binding protein have been associated with hypertrophic cardiomyopathy. However, hundreds of variants are known and many have low penetrance and are often found in control populations. Herein, we focused on novel missense variants in phospholamban, an Ala
MeSH term(s)	Child, Preschool ; Female ; Humans ; Middle Aged ; Calcium/metabolism ; Calcium-Binding Proteins/genetics ; Calcium-Binding Proteins/metabolism ; Cardiac Myosins/genetics ; Cardiac Myosins/metabolism ; Cardiomyopathy, Dilated/diagnosis ; Cardiomyopathy, Dilated/genetics ; Cardiomyopathy, Dilated/metabolism ; Peptides/metabolism ; Carrier Proteins/genetics ; Carrier Proteins/metabolism
Chemical Substances	Calcium (SY7Q814VUP) ; Calcium-Binding Proteins ; Cardiac Myosins (EC 3.6.1.-) ; Peptides ; phospholamban ; myosin-binding protein C ; Carrier Proteins
Language	English
Publishing date	2024-02-22
Publishing country	Netherlands
Document type	Case Reports ; Journal Article ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2024.119699
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Article ; Online: Functional Role of an Unusual Transmembrane Acidic Residue in the Calcium Pump Regulator Myoregulin.

Liu, Andy Y / Rathod, Nishadh / Guerrero-Serna, Guadalupe / Young, Howard S / Espinoza-Fonseca, L Michel

Biochemistry

2023 Volume 62, Issue 8, Page(s) 1331–1336

Abstract: Myoregulin (MLN) is a member of the regulin family, a group of homologous membrane proteins that bind to and regulate the activity of the sarcoplasmic reticulum ... ...

Abstract	Myoregulin (MLN) is a member of the regulin family, a group of homologous membrane proteins that bind to and regulate the activity of the sarcoplasmic reticulum Ca
MeSH term(s)	Calcium/metabolism ; Calcium-Binding Proteins/chemistry ; Ion Transport ; Molecular Conformation ; Muscle, Skeletal/metabolism ; Sarcoplasmic Reticulum/chemistry ; Sarcoplasmic Reticulum/metabolism ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/chemistry ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism ; Humans
Chemical Substances	Calcium (SY7Q814VUP) ; Calcium-Binding Proteins ; Sarcoplasmic Reticulum Calcium-Transporting ATPases (EC 3.6.3.8)
Language	English
Publishing date	2023-04-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.3c00026
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Article ; Online: Regulating the regulator: intramembrane proteolysis of vesicular trafficking proteins and the SERCA regulator phospholamban.

Young, Howard S / Lemieux, M Joanne

EMBO reports

2019 Volume 20, Issue 3

Language	English
Publishing date	2019-02-25
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.201947792
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Article ; Online: Replacement of Lys27 by asparagine in the SERCA regulator myoregulin: A Ca

Rathod, Nishadh / Guerrero-Serna, Guadalupe / Young, Howard S / Espinoza-Fonseca, L Michel

Biochimica et biophysica acta. Molecular cell research

2023 Volume 1871, Issue 1, Page(s) 119613

Abstract: Myoregulin (MLN) is a protein that regulates the activity of the sarcoplasmic reticulum ... ...

Abstract	Myoregulin (MLN) is a protein that regulates the activity of the sarcoplasmic reticulum Ca
MeSH term(s)	Asparagine/metabolism ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/genetics ; Sarcoplasmic Reticulum/metabolism
Chemical Substances	Asparagine (7006-34-0) ; Sarcoplasmic Reticulum Calcium-Transporting ATPases (EC 3.6.3.8)
Language	English
Publishing date	2023-11-02
Publishing country	Netherlands
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2023.119613
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Article ; Online: Helical Membrane Protein Crystallization in the New Era of Electron Cryo-Microscopy.

Hernando, Mary D / Primeau, Joseph O / Young, Howard S

Methods in molecular biology (Clifton, N.J.)

2021 Volume 2302, Page(s) 179–199

Abstract: Helical assemblies of proteins, which consist of a two-dimensional lattice of identical subunits arranged with helical symmetry, are a common structural motif in nature. For membrane proteins, crystallization protocols can induce helical arrangements and ...

Abstract	Helical assemblies of proteins, which consist of a two-dimensional lattice of identical subunits arranged with helical symmetry, are a common structural motif in nature. For membrane proteins, crystallization protocols can induce helical arrangements and take advantage of the symmetry found in these assemblies for the structural determination of target proteins. Modern advances in the field of electron cryo-microscopy (cryo-EM), in particular the advent of direct electron detectors, have opened the potential for structure determination of membrane proteins in such assemblies at high resolution. The nature of the symmetry in helical crystals of membrane proteins means that a single image potentially contains enough information for three-dimensional structural determination. With the current direct electron detectors, we have never been closer to making this a reality. Here, we present a protocol detailing the preparation of helical crystals, with an emphasis on further cryo-EM analysis and structural determination of the sarco(endo)plasmic reticulum Ca
MeSH term(s)	Algorithms ; Calcium-Binding Proteins/chemistry ; Calcium-Binding Proteins/metabolism ; Computational Biology ; Cryoelectron Microscopy ; Crystallization ; Models, Molecular ; Protein Conformation, alpha-Helical ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/chemistry ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism
Chemical Substances	Calcium-Binding Proteins ; phospholamban ; Sarcoplasmic Reticulum Calcium-Transporting ATPases (EC 3.6.3.8)
Language	English
Publishing date	2021-04-20
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-1394-8_10
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Article ; Online: Skin cells prefer a slower calcium pump.

Robia, Seth L / Young, Howard S

The Journal of biological chemistry

2018 Volume 293, Issue 11, Page(s) 3890–3891

Abstract: Naturally occurring mutations of a calcium ion transporter can cause a skin condition known as Darier's disease. In this issue of JBC, ... ...

Abstract	Naturally occurring mutations of a calcium ion transporter can cause a skin condition known as Darier's disease. In this issue of JBC, Mikkelsen
MeSH term(s)	Calcium/metabolism ; Calcium Signaling ; Darier Disease/genetics ; Darier Disease/pathology ; Humans ; Kinetics ; Mutation ; Protein Conformation ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/chemistry ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/genetics ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism
Chemical Substances	Sarcoplasmic Reticulum Calcium-Transporting ATPases (EC 3.6.3.8) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2018-04-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.H118.002088
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Article ; Online: Stimulation of Ca

Sordi, Giacomo / Goti, Andrea / Young, Howard S / Palchetti, Ilaria / Tadini-Buoninsegni, Francesco

ChemMedChem

2021 Volume 16, Issue 21, Page(s) 3293–3299

Abstract: The sarco(endo)plasmic reticulum ... ...

Abstract	The sarco(endo)plasmic reticulum Ca
MeSH term(s)	Aminoquinolines/chemistry ; Aminoquinolines/pharmacology ; Benzamides/chemistry ; Benzamides/pharmacology ; Dose-Response Relationship, Drug ; Humans ; Molecular Structure ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism ; Small Molecule Libraries/chemistry ; Small Molecule Libraries/pharmacology ; Structure-Activity Relationship
Chemical Substances	Aminoquinolines ; Benzamides ; CDN1163 ; Small Molecule Libraries ; Sarcoplasmic Reticulum Calcium-Transporting ATPases (EC 3.6.3.8)
Language	English
Publishing date	2021-08-26
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2218496-X
ISSN	1860-7187 ; 1860-7179
ISSN (online)	1860-7187
ISSN	1860-7179
DOI	10.1002/cmdc.202100350
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Article: Structure-Function Relationship of the SERCA Pump and Its Regulation by Phospholamban and Sarcolipin.

Gorski, Przemek A / Ceholski, Delaine K / Young, Howard S

Advances in experimental medicine and biology

2018 Volume 981, Page(s) 77–119

Abstract: Calcium is a universal second messenger involved in diverse cellular processes, including excitation-contraction coupling in muscle. The contraction and relaxation of cardiac muscle cells are regulated by the cyclic movement of calcium primarily between ... ...

Abstract	Calcium is a universal second messenger involved in diverse cellular processes, including excitation-contraction coupling in muscle. The contraction and relaxation of cardiac muscle cells are regulated by the cyclic movement of calcium primarily between the extracellular space, the cytoplasm and the sarcoplasmic reticulum (SR). The rapid removal of calcium from the cytosol is primarily facilitated by the sarco(endo)plasmic reticulum calcium ATPase (SERCA) which pumps calcium back into the SR lumen and thereby controls the amount of calcium in the SR. The most studied member of the P-type ATPase family, SERCA has multiple tissue- and cell-specific isoforms and is primarily regulated by two peptides in muscle, phospholamban and sarcolipin. The multifaceted regulation of SERCA via these peptides is exemplified in the biological fine-tuning of their independent oligomerization and regulation. In this chapter, we overview the structure-function relationship of SERCA and its peptide modulators, detailing the regulation of the complexes and summarizing their physiological and disease relevance.
MeSH term(s)	Animals ; Calcium/chemistry ; Calcium/metabolism ; Calcium-Binding Proteins/chemistry ; Calcium-Binding Proteins/metabolism ; Cytosol/chemistry ; Cytosol/metabolism ; Humans ; Muscle Proteins/chemistry ; Muscle Proteins/metabolism ; Organ Specificity ; Proteolipids/chemistry ; Proteolipids/metabolism ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/chemistry ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism ; Structure-Activity Relationship
Chemical Substances	Calcium-Binding Proteins ; Muscle Proteins ; Proteolipids ; phospholamban ; sarcolipin (145018-73-1) ; Sarcoplasmic Reticulum Calcium-Transporting ATPases (EC 3.6.3.8) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2018-03-28
Publishing country	United States
Document type	Journal Article ; Review
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-3-319-55858-5_5
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Article ; Online: Protein docking and steered molecular dynamics suggest alternative phospholamban-binding sites on the SERCA calcium transporter.

Alford, Rebecca F / Smolin, Nikolai / Young, Howard S / Gray, Jeffrey J / Robia, Seth L

The Journal of biological chemistry

2020 Volume 295, Issue 32, Page(s) 11262–11274

Abstract: The transport activity of the sarco(endo)plasmic reticulum calcium ATPase (SERCA) in cardiac myocytes is modulated by an inhibitory interaction with a transmembrane peptide, phospholamban (PLB). Previous biochemical studies have revealed that PLB ... ...

Abstract	The transport activity of the sarco(endo)plasmic reticulum calcium ATPase (SERCA) in cardiac myocytes is modulated by an inhibitory interaction with a transmembrane peptide, phospholamban (PLB). Previous biochemical studies have revealed that PLB interacts with a specific inhibitory site on SERCA, and low-resolution structural evidence suggests that PLB interacts with distinct alternative sites on SERCA. High-resolution details of the structural determinants of SERCA regulation have been elusive because of the dynamic nature of the regulatory complex. In this study, we used computational approaches to develop a structural model of SERCA-PLB interactions to gain a mechanistic understanding of PLB-mediated SERCA transport regulation. We combined steered molecular dynamics and membrane protein-protein docking experiments to achieve both a global search and all-atom force calculations to determine the relative affinities of PLB for candidate sites on SERCA. We modeled the binding of PLB to several SERCA conformations, representing different enzymatic states sampled during the calcium transport catalytic cycle. The results of the steered molecular dynamics and docking experiments indicated that the canonical PLB-binding site (comprising transmembrane helices M2, M4, and M9) is the preferred site. This preference was even more stringent for a superinhibitory PLB variant. Interestingly, PLB-binding specificity became more ambivalent for other SERCA conformers. These results provide evidence for polymorphic PLB interactions with novel sites on M3 and with the outside of the SERCA helix M9. Our findings are compatible with previous physical measurements that suggest that PLB interacts with multiple binding sites, conferring dynamic responsiveness to changing physiological conditions.
MeSH term(s)	Animals ; Binding Sites ; Calcium-Binding Proteins/metabolism ; Humans ; Molecular Dynamics Simulation ; Proteins/metabolism ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism
Chemical Substances	Calcium-Binding Proteins ; Proteins ; phospholamban ; Sarcoplasmic Reticulum Calcium-Transporting ATPases (EC 3.6.3.8)
Language	English
Publishing date	2020-06-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA120.012948
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Article ; Online: Nothing Regular about the Regulins: Distinct Functional Properties of SERCA Transmembrane Peptide Regulatory Subunits.

Rathod, Nishadh / Bak, Jessi J / Primeau, Joseph O / Fisher, M'Lynn E / Espinoza-Fonseca, Lennane Michel / Lemieux, Mary Joanne / Young, Howard S

International journal of molecular sciences

2021 Volume 22, Issue 16

Abstract: The sarco-endoplasmic reticulum calcium ATPase (SERCA) is responsible for maintaining calcium homeostasis in all eukaryotic cells by actively transporting calcium from the cytosol into the sarco-endoplasmic reticulum (SR/ER) lumen. Calcium is an ... ...

Abstract	The sarco-endoplasmic reticulum calcium ATPase (SERCA) is responsible for maintaining calcium homeostasis in all eukaryotic cells by actively transporting calcium from the cytosol into the sarco-endoplasmic reticulum (SR/ER) lumen. Calcium is an important signaling ion, and the activity of SERCA is critical for a variety of cellular processes such as muscle contraction, neuronal activity, and energy metabolism. SERCA is regulated by several small transmembrane peptide subunits that are collectively known as the "regulins". Phospholamban (PLN) and sarcolipin (SLN) are the original and most extensively studied members of the regulin family. PLN and SLN inhibit the calcium transport properties of SERCA and they are required for the proper functioning of cardiac and skeletal muscles, respectively. Myoregulin (MLN), dwarf open reading frame (DWORF), endoregulin (ELN), and another-regulin (ALN) are newly discovered tissue-specific regulators of SERCA. Herein, we compare the functional properties of the regulin family of SERCA transmembrane peptide subunits and consider their regulatory mechanisms in the context of the physiological and pathophysiological roles of these peptides. We present new functional data for human MLN, ELN, and ALN, demonstrating that they are inhibitors of SERCA with distinct functional consequences. Molecular modeling and molecular dynamics simulations of SERCA in complex with the transmembrane domains of MLN and ALN provide insights into how differential binding to the so-called inhibitory groove of SERCA-formed by transmembrane helices M2, M6, and M9-can result in distinct functional outcomes.
MeSH term(s)	Animals ; Calcium/metabolism ; Calcium-Binding Proteins/genetics ; Calcium-Binding Proteins/metabolism ; Humans ; Models, Molecular ; Muscle Proteins/genetics ; Muscle Proteins/metabolism ; Proteolipids/genetics ; Proteolipids/metabolism ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/genetics ; Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism
Chemical Substances	Calcium-Binding Proteins ; Muscle Proteins ; Proteolipids ; myoregulin, human ; phospholamban ; sarcolipin (145018-73-1) ; Sarcoplasmic Reticulum Calcium-Transporting ATPases (EC 3.6.3.8) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2021-08-18
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms22168891
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