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Article ; Online: John Squire and the myosin thick filament structure in muscle.

Taylor, Kenneth A

Journal of muscle research and cell motility

2023 Volume 44, Issue 3, Page(s) 143–152

Abstract: The structure of the thin, actin-containing filament of muscle is both highly conserved across a broad range of muscle types and is now well understood. The structure of the thick, myosin-containing filaments of striated muscle are quite variable and ... ...

Abstract	The structure of the thin, actin-containing filament of muscle is both highly conserved across a broad range of muscle types and is now well understood. The structure of the thick, myosin-containing filaments of striated muscle are quite variable and remained comparatively unknown until recently, particularly in the arrangement of the myosin tails. John Squire played a major role not only in our understanding of thin filament structure and function but also in the structure of the thick filaments. Long before much was known about the structure and composition of muscle thick filaments, he proposed a general model for how myosin filaments were constructed. His role in our current understanding the structure of striated muscle thick filaments and the extent through which his predictions have held true is the topic of this review.
MeSH term(s)	Myosins/chemistry ; Sarcomeres ; Muscle, Skeletal ; Actin Cytoskeleton
Chemical Substances	Myosins (EC 3.6.4.1)
Language	English
Publishing date	2023-04-26
Publishing country	Netherlands
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	283053-x
ISSN	1573-2657 ; 0142-4319
ISSN (online)	1573-2657
ISSN	0142-4319
DOI	10.1007/s10974-023-09646-4
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Article ; Online: Identifying characteristics and clinical conditions associated with hand grip strength in adults: the Project Baseline Health Study.

Taylor, Kenneth A / Carroll, Megan K / Short, Sarah A / Goode, Adam P

Scientific reports

2024 Volume 14, Issue 1, Page(s) 8937

Abstract: Low hand grip strength (HGS) is associated with several conditions, but its value outside of the older adult population is unclear. We sought to identify the most salient factors associated with HGS from an extensive list of candidate variables while ... ...

Abstract	Low hand grip strength (HGS) is associated with several conditions, but its value outside of the older adult population is unclear. We sought to identify the most salient factors associated with HGS from an extensive list of candidate variables while stratifying by age and sex. We used data from the initial visit from the Project Baseline Health Study (N = 2502) which captured detailed demographic, occupational, social, lifestyle, and clinical data. We applied MI-LASSO using group methods to determine variables most associated with HGS out of 175 candidate variables. We performed analyses separately for sex and age (< 65 vs. ≥ 65 years). Race was associated with HGS to varying degrees across groups. Osteoporosis and osteopenia were negatively associated with HGS in female study participants. Immune cell counts were negatively associated with HGS for male participants ≥ 65 (neutrophils) and female participants (≥ 65, monocytes; < 65, lymphocytes). Most findings were age and/or sex group-specific; few were common across all groups. Several of the variables associated with HGS in each group were novel, while others corroborate previous research. Our results support HGS as a useful indicator of a variety of clinical characteristics; however, its utility varies by age and sex.
MeSH term(s)	Humans ; Male ; Female ; Aged ; Hand Strength ; Life Style ; Reference Values ; Sex Factors
Language	English
Publishing date	2024-04-18
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-024-55978-7
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Article ; Online: Structure of mavacamten-free human cardiac thick filaments within the sarcomere by cryoelectron tomography.

Chen, Liang / Liu, Jun / Rastegarpouyani, Hosna / Janssen, Paul M L / Pinto, Jose R / Taylor, Kenneth A

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

2024 Volume 121, Issue 9, Page(s) e2311883121

Abstract: Heart muscle has the unique property that it can never rest; all cardiomyocytes contract with each heartbeat which requires a complex control mechanism to regulate cardiac output to physiological requirements. Changes in calcium concentration regulate ... ...

Abstract	Heart muscle has the unique property that it can never rest; all cardiomyocytes contract with each heartbeat which requires a complex control mechanism to regulate cardiac output to physiological requirements. Changes in calcium concentration regulate the thin filament activation. A separate but linked mechanism regulates the thick filament activation, which frees sufficient myosin heads to bind the thin filament, thereby producing the required force. Thick filaments contain additional nonmyosin proteins, myosin-binding protein C and titin, the latter being the protein that transmits applied tension to the thick filament. How these three proteins interact to control thick filament activation is poorly understood. Here, we show using 3-D image reconstruction of frozen-hydrated human cardiac muscle myofibrils lacking exogenous drugs that the thick filament is structured to provide three levels of myosin activation corresponding to the three crowns of myosin heads in each 429Å repeat. In one crown, the myosin heads are almost completely activated and disordered. In another crown, many myosin heads are inactive, ordered into a structure called the interacting heads motif. At the third crown, the myosin heads are ordered into the interacting heads motif, but the stability of that motif is affected by myosin-binding protein C. We think that this hierarchy of control explains many of the effects of length-dependent activation as well as stretch activation in cardiac muscle control.
MeSH term(s)	Humans ; Sarcomeres ; Myocardium ; Myofibrils ; Myocytes, Cardiac ; Myosins ; Benzylamines ; Uracil/analogs & derivatives
Chemical Substances	MYK-461 ; Myosins (EC 3.6.4.1) ; Benzylamines ; Uracil (56HH86ZVCT)
Language	English
Publishing date	2024-02-22
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.2311883121
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Article ; Online: Structure of the

Abbasi Yeganeh, Fatemeh / Rastegarpouyani, Hosna / Li, Jiawei / Taylor, Kenneth A

International journal of molecular sciences

2023 Volume 24, Issue 19

Abstract: Striated muscle thick filaments are composed of myosin II and several non-myosin proteins which define the filament length and modify its function. Myosin II has a globular N-terminal motor domain comprising its catalytic and actin-binding activities and ...

Abstract	Striated muscle thick filaments are composed of myosin II and several non-myosin proteins which define the filament length and modify its function. Myosin II has a globular N-terminal motor domain comprising its catalytic and actin-binding activities and a long α-helical, coiled tail that forms the dense filament backbone. Myosin alone polymerizes into filaments of irregular length, but striated muscle thick filaments have defined lengths that, with thin filaments, define the sarcomere structure. The motor domain structure and function are well understood, but the myosin filament backbone is not. Here we report on the structure of the flight muscle thick filaments from
MeSH term(s)	Animals ; Drosophila melanogaster/genetics ; Muscle Proteins/metabolism ; Muscle, Skeletal/metabolism ; Filamins/metabolism ; Myosins/metabolism ; Drosophila Proteins/metabolism ; Drosophila/metabolism ; Myosin Type II/metabolism
Chemical Substances	Muscle Proteins ; Filamins ; Myosins (EC 3.6.4.1) ; Drosophila Proteins ; Myosin Type II (EC 3.6.1.-)
Language	English
Publishing date	2023-10-05
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms241914936
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Article ; Online: Novel ADP State Found in Smooth Muscle Heavy Meromyosin by CryoEM.

Hojjatian, Alimohammad / Rastegarpouyani, Hosna / Taylor, Dianne W / Taylor, Kenneth A

Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada

2023 Volume 29, Issue 29 Suppl 1, Page(s) 912–914

Language	English
Publishing date	2023-08-23
Publishing country	England
Document type	Journal Article
ZDB-ID	1385710-1
ISSN	1435-8115 ; 1431-9276
ISSN (online)	1435-8115
ISSN	1431-9276
DOI	10.1093/micmic/ozad067.452
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Article ; Online: Optimizing the Protein Stability in Thick Filament Cryo-EM Sample Preparation Using a PEGylation Technique.

Rastegarpouyani, Hosna / Yeganeh, Fatemeh Abbasi / Hojjatian, Alimohammad / Taylor, Kenneth A

Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada

2023 Volume 29, Issue 29 Suppl 1, Page(s) 958–959

Language	English
Publishing date	2023-08-24
Publishing country	England
Document type	Journal Article
ZDB-ID	1385710-1
ISSN	1435-8115 ; 1431-9276
ISSN (online)	1435-8115
ISSN	1431-9276
DOI	10.1093/micmic/ozad067.478
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Article ; Online: Probable trauma associated sleep disorder in post-9/11 US Veterans.

Taylor, Kenneth A / Mysliwiec, Vincent / Kimbrel, Nathan A / Augustine, Ann V / Ulmer, Christi S

Sleep advances : a journal of the Sleep Research Society

2023 Volume 4, Issue 1, Page(s) zpad001

Abstract: Study objectives: The purpose of this study was to (1) estimate trauma associated sleep disorder (TASD) prevalence among post-9/11 era veterans and to describe differences in service and comorbid mental health clinical characteristics among individuals ... ...

Abstract	Study objectives: The purpose of this study was to (1) estimate trauma associated sleep disorder (TASD) prevalence among post-9/11 era veterans and to describe differences in service and comorbid mental health clinical characteristics among individuals with and without probable TASD, and (2) estimate TASD prevalence and characteristics of reported traumatic experiences stratified by sex. Methods: We used cross-sectional data from the post-deployment mental health study of post-9/11 veterans, which enrolled and collected baseline data from 2005 to 2018. We classified veterans as having probable TASD using self-reported measures: traumatic experiences from the traumatic life events questionnaire (TLEQ) and items from the Pittsburgh sleep quality index with Addendum for posttraumatic stress disorder (PTSD) mapped to TASD diagnostic criteria and ascertained mental health diagnoses (PTSD, major depressive disorder [MDD]) via Structured Clinical Interview for Results: Our final sample included 3618 veterans (22.7% female). TASD prevalence was 12.1% (95% CI: 11.1% to 13.2%) and sex-stratified prevalence was similar for female and male veterans. Veterans with TASD had a much higher comorbid prevalence of PTSD (PR: 3.72, 95% CI: 3.41 to 4.06) and MDD (PR: 3.93, 95% CI: 3.48 to 4.43). Combat was the highest reported most distressing traumatic experience among veterans with TASD (62.6%). When stratifying by sex, female veterans with TASD had a wider variety of traumatic experiences. Conclusions: Our results support the need for improved screening and evaluation for TASD in veterans, which is currently not performed in routine clinical practice.
Language	English
Publishing date	2023-01-12
Publishing country	United States
Document type	Journal Article
ISSN	2632-5012
ISSN (online)	2632-5012
DOI	10.1093/sleepadvances/zpad001
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Article ; Online: Double-headed binding of myosin II to F-actin shows the effect of strain on head structure.

Hojjatian, Alimohammad / Taylor, Dianne W / Daneshparvar, Nadia / Fagnant, Patricia M / Trybus, Kathleen M / Taylor, Kenneth A

Journal of structural biology

2023 Volume 215, Issue 3, Page(s) 107995

Abstract: Force production in muscle is achieved through the interaction of myosin and actin. Strong binding states in active muscle are associated with Mg·ADP bound to the active site; release of Mg·ADP allows rebinding of ATP and dissociation from actin. Thus, ... ...

Abstract	Force production in muscle is achieved through the interaction of myosin and actin. Strong binding states in active muscle are associated with Mg·ADP bound to the active site; release of Mg·ADP allows rebinding of ATP and dissociation from actin. Thus, Mg·ADP binding is positioned for adaptation as a force sensor. Mechanical loads on the lever arm can affect the ability of myosin to release Mg·ADP but exactly how this is done is poorly defined. Here we use F-actin decorated with double-headed smooth muscle myosin fragments in the presence of Mg·ADP to visualize the effect of internally supplied tension on the paired lever arms using cryoEM. The interaction of the paired heads with two adjacent actin subunits is predicted to place one lever arm under positive and the other under negative strain. The converter domain is believed to be the most flexible domain within myosin head. Our results, instead, point to the segment of heavy chain between the essential and regulatory light chains as the location of the largest structural change. Moreover, our results suggest no large changes in the myosin coiled coil tail as the locus of strain relief when both heads bind F-actin. The method would be adaptable to double-headed members of the myosin family. We anticipate that the study of actin-myosin interaction using double-headed fragments enables visualization of domains that are typically noisy in decoration with single-headed fragments.
MeSH term(s)	Actins/metabolism ; Myosins/chemistry ; Myosin Type II/analysis ; Actin Cytoskeleton/metabolism ; Muscle, Skeletal/chemistry
Chemical Substances	Actins ; Myosins (EC 3.6.4.1) ; Myosin Type II (EC 3.6.1.-)
Language	English
Publishing date	2023-07-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1032718-6
ISSN	1095-8657 ; 1047-8477
ISSN (online)	1095-8657
ISSN	1047-8477
DOI	10.1016/j.jsb.2023.107995
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Zs.A 1428: Show issues

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Article ; Online: The cryo-EM 3D image reconstruction of isolated Lethocerus indicus Z-discs.

Yeganeh, Fatemeh Abbasi / Summerill, Corinne / Hu, Zhongjun / Rahmani, Hamidreza / Taylor, Dianne W / Taylor, Kenneth A

Journal of muscle research and cell motility

2023 Volume 44, Issue 4, Page(s) 271–286

Abstract: The Z-disk of striated muscle defines the ends of the sarcomere, which repeats many times within the muscle fiber. Here we report application of cryoelectron tomography and subtomogram averaging to Z-disks isolated from the flight muscles of the large ... ...

Abstract	The Z-disk of striated muscle defines the ends of the sarcomere, which repeats many times within the muscle fiber. Here we report application of cryoelectron tomography and subtomogram averaging to Z-disks isolated from the flight muscles of the large waterbug Lethocerus indicus. We use high salt solutions to remove the myosin containing filaments and use gelsolin to remove the actin filaments of the A- and I-bands leaving only the thin filaments within the Z-disk which were then frozen for cryoelectron microscopy. The Lethocerus Z-disk structure is similar in many ways to the previously studied Z-disk of the honeybee Apis mellifera. At the corners of the unit cell are positioned trimers of paired antiparallel F-actins defining a large solvent channel, whereas at the trigonal positions are positioned F-actin trimers converging slowly towards their (+) ends defining a small solvent channel through the Z-disk. These near parallel F-actins terminate at different Z-heights within the Z-disk. The two types of solvent channel in Lethocerus are similar in size compared to those of Apis which are very different in size. Two types of α-actinin crosslinks were observed between oppositely oriented actin filaments. In one of these, the α-actinin long axis is almost parallel to the F-actins it crosslinks. In the other, the α-actinins are at a small but distinctive angle with respect to the crosslinked actin filaments. The utility of isolated Z-disks for structure determination is discussed.
MeSH term(s)	Animals ; Sarcomeres/metabolism ; Actins/metabolism ; Actinin/metabolism ; Muscle Proteins/metabolism ; Cryoelectron Microscopy ; Muscle, Skeletal/metabolism ; Solvents/metabolism ; Image Processing, Computer-Assisted
Chemical Substances	Actins ; Actinin (11003-00-2) ; Muscle Proteins ; Solvents
Language	English
Publishing date	2023-09-03
Publishing country	Netherlands
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	283053-x
ISSN	1573-2657 ; 0142-4319
ISSN (online)	1573-2657
ISSN	0142-4319
DOI	10.1007/s10974-023-09657-1
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Article ; Online: John Squire: a leader and seminal contributor to experimental and theoretical muscle research for over 50 years.

Luther, Pradeep K / Morris, Edward P / Parry, David A D / Taylor, Kenneth A

Journal of muscle research and cell motility

2023 Volume 44, Issue 3, Page(s) 123–124

Language	English
Publishing date	2023-09-22
Publishing country	Netherlands
Document type	Editorial
ZDB-ID	283053-x
ISSN	1573-2657 ; 0142-4319
ISSN (online)	1573-2657
ISSN	0142-4319
DOI	10.1007/s10974-023-09659-z
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