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Article: FHODs: Nuclear tethered formins for nuclear mechanotransduction.

Antoku, Susumu / Schwartz, Thomas U / Gundersen, Gregg G

Frontiers in cell and developmental biology

2023 Volume 11, Page(s) 1160219

Abstract: In this review, we discuss FHOD formins with a focus on recent studies that reveal a new role for them as critical links for nuclear mechanotransduction. The FHOD family in vertebrates comprises two structurally related proteins, FHOD1 ... ...

Abstract	In this review, we discuss FHOD formins with a focus on recent studies that reveal a new role for them as critical links for nuclear mechanotransduction. The FHOD family in vertebrates comprises two structurally related proteins, FHOD1 and
Language	English
Publishing date	2023-05-04
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2023.1160219
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Article ; Online: Analysis of Nesprin-2 Interaction with Its Binding Partners and Actin.

Antoku, Susumu / Gundersen, Gregg G

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

2018 Volume 1840, Page(s) 35–43

Abstract: Nuclei are connected to the actin cytoskeleton for controlling its position in the cell and for mechanochemical signaling. Nesprin-2G is one of the major outer nuclear membrane proteins that links the nucleus to the actin cytoskeleton. In addition to its ...

Abstract	Nuclei are connected to the actin cytoskeleton for controlling its position in the cell and for mechanochemical signaling. Nesprin-2G is one of the major outer nuclear membrane proteins that links the nucleus to the actin cytoskeleton. In addition to its paired calponin homology (CH) domains, nesprin-2G interacts with actin filaments by binding the actin-bundling proteins FHOD1 and fascin. We describe methods to measure the interaction of nesprin-2G with actin filaments using an actin co-sedimentation assay and with its binding partner FHOD1 using a GST pull-down method.
MeSH term(s)	Actins/metabolism ; Animals ; Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Fetal Proteins/chemistry ; Fetal Proteins/metabolism ; Humans ; Mice ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/metabolism ; Nuclear Proteins/chemistry ; Nuclear Proteins/metabolism ; Protein Binding ; Protein Interaction Domains and Motifs ; Recombinant Fusion Proteins
Chemical Substances	Actins ; Carrier Proteins ; FHOD1 protein, mouse ; Fetal Proteins ; Nerve Tissue Proteins ; Nuclear Proteins ; Recombinant Fusion Proteins ; Syne2 protein, mouse
Language	English
Publishing date	2018-09-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-8691-0_4
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Article ; Online: Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins.

Lim, Sing Mei / Cruz, Victor E / Antoku, Susumu / Gundersen, Gregg G / Schwartz, Thomas U

Structure (London, England : 1993)

2021 Volume 29, Issue 6, Page(s) 540–552.e5

Abstract: The nuclear position in eukaryotes is controlled by a nucleo-cytoskeletal network, critical in cell differentiation, division, and movement. Forces are transmitted through conserved Linker of Nucleoskeleton and Cytoskeleton (LINC) complexes that traverse ...

Abstract	The nuclear position in eukaryotes is controlled by a nucleo-cytoskeletal network, critical in cell differentiation, division, and movement. Forces are transmitted through conserved Linker of Nucleoskeleton and Cytoskeleton (LINC) complexes that traverse the nuclear envelope and engage on either side of the membrane with diverse binding partners. Nesprin-2-giant (Nes2G), a LINC element in the outer nuclear membrane, connects to the actin directly as well as through FHOD1, a formin primarily involved in actin bundling. Here, we report the crystal structure of Nes2G bound to FHOD1 and show that the presumed G-binding domain of FHOD1 is rather a spectrin repeat (SR) binding enhancer for the neighboring FH3 domain. The structure reveals that SR binding by FHOD1 is likely not regulated by the diaphanous-autoregulatory domain helix of FHOD1. Finally, we establish that Nes1G also has one FHOD1 binding SR, indicating that these abundant, giant Nesprins have overlapping functions in actin-bundle recruitment for nuclear movement.
MeSH term(s)	Amino Acid Motifs ; Animals ; Crystallography, X-Ray ; Cytoskeletal Proteins/chemistry ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Fetal Proteins/chemistry ; Fetal Proteins/metabolism ; Formins/chemistry ; Formins/metabolism ; HEK293 Cells ; Humans ; Mice ; Microfilament Proteins/chemistry ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Models, Molecular ; NIH 3T3 Cells ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Protein Binding ; Protein Conformation ; Protein Domains
Chemical Substances	Cytoskeletal Proteins ; FHOD1 protein, human ; Fetal Proteins ; Formins ; Microfilament Proteins ; Nerve Tissue Proteins ; SYNE1 protein, human ; SYNE2 protein, human
Language	English
Publishing date	2021-01-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2020.12.013
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Article ; Online: Centrifugal Displacement of Nuclei Reveals Multiple LINC Complex Mechanisms for Homeostatic Nuclear Positioning.

Zhu, Ruijun / Antoku, Susumu / Gundersen, Gregg G

Current biology : CB

2017 Volume 27, Issue 20, Page(s) 3097–3110.e5

Abstract: Nuclear movement is critical for developmental events, cell polarity, and migration and is usually mediated by linker of nucleoskeleton and cytoskeleton (LINC) complexes connecting the nucleus to cytoskeletal elements. Compared to active nuclear movement, ...

Abstract	Nuclear movement is critical for developmental events, cell polarity, and migration and is usually mediated by linker of nucleoskeleton and cytoskeleton (LINC) complexes connecting the nucleus to cytoskeletal elements. Compared to active nuclear movement, relatively little is known about homeostatic positioning of nuclei, including whether it is an active process. To explore homeostatic nuclear positioning, we developed a method to displace nuclei in adherent cells using centrifugal force. Nuclei displaced by centrifugation rapidly recentered by mechanisms that depended on cell context. In cell monolayers with wounds oriented orthogonal to the force, nuclei were displaced toward the front and back of the cells on the two sides of the wound. Nuclei recentered from both positions, but at different rates and with different cytoskeletal linkage mechanisms. Rearward recentering was actomyosin, nesprin-2G, and SUN2 dependent, whereas forward recentering was microtubule, dynein, nesprin-2G, and SUN1 dependent. Nesprin-2G engaged actin through its N terminus and microtubules through a novel dynein interacting site near its C terminus. Both activities were necessary to maintain nuclear position in uncentrifuged cells. Thus, even when not moving, nuclei are actively maintained in position by engaging the cytoskeleton through the LINC complex.
MeSH term(s)	Cell Line ; Cell Movement/physiology ; Cell Nucleus/physiology ; Homeostasis ; Humans ; Intracellular Signaling Peptides and Proteins/metabolism
Chemical Substances	Intracellular Signaling Peptides and Proteins
Language	English
Publishing date	2017-10-05
Publishing country	England
Document type	Journal Article
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2017.08.073
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Article ; Online: Wound-Healing Assays to Study Mechanisms of Nuclear Movement in Fibroblasts and Myoblasts.

Chang, Wakam / Antoku, Susumu / Gundersen, Gregg G

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

2016 Volume 1411, Page(s) 255–267

Abstract: The rearward positioning of the nucleus is a characteristic feature of most migrating cells. Studies using wounded monolayers of fibroblasts and myoblasts have shown that this positioning is actively established before migration by the coupling of dorsal ...

Abstract	The rearward positioning of the nucleus is a characteristic feature of most migrating cells. Studies using wounded monolayers of fibroblasts and myoblasts have shown that this positioning is actively established before migration by the coupling of dorsal actin cables to the nuclear envelope through nesprin-2G and SUN2 linker of nucleoskeleton and cytoskeleton (LINC) complexes. During nuclear movement, these LINC complexes cluster along the actin cables to form adhesive structures known as transmembrane actin-associated nuclear (TAN) lines. Here we described experimental procedures for studying nuclear movement and TAN lines using wounded monolayers of fibroblasts and myoblasts, the acquisition of data using immunofluorescence microscopy and live-cell imaging, and methods for data analysis and quantification.
Language	English
Publishing date	2016
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-3530-7_17
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Article ; Online: ERK1/2 Phosphorylation of FHOD Connects Signaling and Nuclear Positioning Alternations in Cardiac Laminopathy.

Antoku, Susumu / Wu, Wei / Joseph, Leroy C / Morrow, John P / Worman, Howard J / Gundersen, Gregg G

Developmental cell

2019 Volume 51, Issue 5, Page(s) 602–616.e12

Abstract: Mutations in the lamin A/C gene (LMNA) cause cardiomyopathy and also disrupt nuclear positioning in fibroblasts. LMNA mutations causing cardiomyopathy elevate ERK1/2 activity in the heart, and inhibition of the ERK1/2 kinase activity ameliorates ... ...

Abstract	Mutations in the lamin A/C gene (LMNA) cause cardiomyopathy and also disrupt nuclear positioning in fibroblasts. LMNA mutations causing cardiomyopathy elevate ERK1/2 activity in the heart, and inhibition of the ERK1/2 kinase activity ameliorates pathology, but the downstream effectors remain largely unknown. We now show that cardiomyocytes from mice with an Lmna mutation and elevated cardiac ERK1/2 activity have altered nuclear positioning. In fibroblasts, ERK1/2 activation negatively regulated nuclear movement by phosphorylating S498 of FHOD1. Expression of an unphosphorylatable FHOD1 variant rescued the nuclear movement defect in fibroblasts expressing a cardiomyopathy-causing lamin A mutant. In hearts of mice with LMNA mutation-induced cardiomyopathy, ERK1/2 mediated phosphorylation of FHOD3, an isoform highly expressed in cardiac tissue. Phosphorylation of FHOD1 and FHOD3 inhibited their actin bundling activity. These results show that phosphorylation of FHOD proteins by ERK1/2 is a critical switch for nuclear positioning and may play a role in the pathogenesis of cardiomyopathy caused by LMNA mutations.
MeSH term(s)	3T3 Cells ; Actins/metabolism ; Active Transport, Cell Nucleus ; Animals ; Cardiomyopathy, Dilated/genetics ; Cardiomyopathy, Dilated/metabolism ; Cell Nucleus/metabolism ; Cells, Cultured ; Fetal Proteins/genetics ; Fetal Proteins/metabolism ; Formins/genetics ; Formins/metabolism ; HEK293 Cells ; Humans ; Lamins/genetics ; MAP Kinase Signaling System ; Male ; Mice ; Mitogen-Activated Protein Kinase 1/genetics ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 3/genetics ; Mitogen-Activated Protein Kinase 3/metabolism ; Mutation ; Myocytes, Cardiac/metabolism ; Myocytes, Cardiac/pathology ; Phosphorylation
Chemical Substances	Actins ; FHOD1 protein, human ; FHOD3 protein, human ; Fetal Proteins ; Formins ; Lamins ; Mitogen-Activated Protein Kinase 1 (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase 3 (EC 2.7.11.24)
Language	English
Publishing date	2019-11-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2019.10.023
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Zs.A 5742: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Distinct roles for Crk adaptor isoforms in actin reorganization induced by extracellular signals.

Antoku, Susumu / Mayer, Bruce J

Journal of cell science

2009 Volume 122, Issue Pt 22, Page(s) 4228–4238

Abstract: Crk family adaptors, consisting of Src homology 2 (SH2) and SH3 protein-binding domains, mediate assembly of protein complexes in signaling. CrkI, an alternately spliced form of Crk, lacks the regulatory phosphorylation site and C-terminal SH3 domain ... ...

Abstract	Crk family adaptors, consisting of Src homology 2 (SH2) and SH3 protein-binding domains, mediate assembly of protein complexes in signaling. CrkI, an alternately spliced form of Crk, lacks the regulatory phosphorylation site and C-terminal SH3 domain present in CrkII and CrkL. We used gene silencing combined with mutational analysis to probe the role of Crk adaptors in platelet-derived growth-factor receptor beta (PDGFbetaR) signaling. We demonstrate that Crk adaptors are required for formation of focal adhesions, and for PDGF-stimulated remodeling of the actin cytoskeleton and cell migration. Crk-dependent signaling is crucial during the early stages of PDGFbetaR activation, whereas its termination by Abl family tyrosine kinases is important for turnover of focal adhesions and progression of dorsal-membrane ruffles. CrkII and CrkL preferentially activate the small GTPase Rac1, whereas variants lacking a functional C-terminal SH3 domain, including CrkI, preferentially activate Rap1. Thus, differences in the activity of Crk isoforms, including their effectors and their ability to be downregulated by phosphorylation, are important for coordinating dynamic changes in the actin cytoskeleton in response to extracellular signals.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Actins/metabolism ; Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cell Line ; Cell Membrane/metabolism ; Cell Movement/physiology ; Focal Adhesions/metabolism ; Gene Silencing ; Humans ; Mice ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Proto-Oncogene Proteins c-abl/metabolism ; Proto-Oncogene Proteins c-crk/genetics ; Proto-Oncogene Proteins c-crk/metabolism ; Rats ; Receptor, Platelet-Derived Growth Factor beta/metabolism ; Signal Transduction/physiology ; rac1 GTP-Binding Protein/metabolism ; rap1 GTP-Binding Proteins/metabolism ; src Homology Domains/physiology
Chemical Substances	Actins ; Adaptor Proteins, Signal Transducing ; CRK protein, human ; CRKL protein ; Nuclear Proteins ; Protein Isoforms ; Proto-Oncogene Proteins c-crk ; Receptor, Platelet-Derived Growth Factor beta (EC 2.7.10.1) ; Proto-Oncogene Proteins c-abl (EC 2.7.10.2) ; rac1 GTP-Binding Protein (EC 3.6.5.2) ; rap1 GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2009-10-27
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.054627
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Zs.A 1200: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article: Distinct roles for Crk adaptor isoforms in actin reorganization induced by extracellular signals

Antoku, Susumu / Mayer, Bruce J

Journal of cell science. 2009 Nov. 15, v. 122, no. 22

2009

Abstract	Crk family adaptors, consisting of Src homology 2 (SH2) and SH3 protein-binding domains, mediate assembly of protein complexes in signaling. CrkI, an alternately spliced form of Crk, lacks the regulatory phosphorylation site and C-terminal SH3 domain present in CrkII and CrkL. We used gene silencing combined with mutational analysis to probe the role of Crk adaptors in platelet-derived growth-factor receptor β (PDGFβR) signaling. We demonstrate that Crk adaptors are required for formation of focal adhesions, and for PDGF-stimulated remodeling of the actin cytoskeleton and cell migration. Crk-dependent signaling is crucial during the early stages of PDGFβR activation, whereas its termination by Abl family tyrosine kinases is important for turnover of focal adhesions and progression of dorsal-membrane ruffles. CrkII and CrkL preferentially activate the small GTPase Rac1, whereas variants lacking a functional C-terminal SH3 domain, including CrkI, preferentially activate Rap1. Thus, differences in the activity of Crk isoforms, including their effectors and their ability to be downregulated by phosphorylation, are important for coordinating dynamic changes in the actin cytoskeleton in response to extracellular signals.
Language	English
Dates of publication	2009-1115
Size	p. 4228-4238.
Publishing place	The Company of Biologists Limited
Document type	Article
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
Database	NAL-Catalogue (AGRICOLA)

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Article: Linker of nucleoskeleton and cytoskeleton (LINC) complex-mediated actin-dependent nuclear positioning orients centrosomes in migrating myoblasts

Chang, Wakam / Antoku, Susumu / Östlund, Cecilia / Worman, Howard J / Gundersen, Gregg G

Nucleus. 2015 Jan. 2, v. 6, no. 1

2015

Abstract: Myoblast migration is essential for muscle development and repair; however, the factors that contribute to the polarity of migrating myoblasts are relatively unknown. We find that randomly migrating C2C12 myoblasts orient their centrosomes in the ... ...

Abstract	Myoblast migration is essential for muscle development and repair; however, the factors that contribute to the polarity of migrating myoblasts are relatively unknown. We find that randomly migrating C2C12 myoblasts orient their centrosomes in the direction of migration. Using wounded monolayers, we further show that centrosome orientation is stimulated by the serum factor lysophosphatidic acid (LPA) and involves the rearward movement of the nucleus while the centrosome is maintained at the cell centroid. The rate of nuclear movement correlated with that of actin retrograde flow and both cytochalasin D and blebbistatin prevented nuclear movement and centrosome orientation. Actin-dependent rearward nuclear movement in fibroblasts is mediated by assembly of nuclear membrane nesprin-2G and SUN2 LINC complexes into transmembrane actin-associated nuclear (TAN) lines anchored by A-type lamins and emerin. In C2C12 myoblasts, depletion of nesprin-2G, SUN2 or lamin A/C prevented nuclear movement and endogenous nesprin-2G and a chimeric GFP-mini-nesprin-2G formed TAN lines during nuclear movement. Depleting nesprin-2G strongly interfered with directed cell migration and reduced the efficiency of myoblast fusion into multinucleated myotubes. Our results show that nuclear movement contributes to centrosome orientation and polarity for efficient migration and fusion of myoblasts. Given that mutations in the genes encoding A-type lamins, nesprin-2 and SUN2 cause Emery-Dreifuss muscular dystrophy and related myopathies, our results have implications for understanding the mechanism of disease pathogenesis.
Keywords	actin ; blood serum ; cell movement ; centrosomes ; cytoskeleton ; fibroblasts ; lysophospholipids ; muscle development ; muscular dystrophy ; myoblasts ; myotubes ; nuclear membrane ; pathogenesis
Language	English
Dates of publication	2015-0102
Size	p. 77-88.
Publishing place	Taylor & Francis
Document type	Article
ZDB-ID	2619626-8
ISSN	1949-1042 ; 1949-1034
ISSN (online)	1949-1042
ISSN	1949-1034
DOI	10.1080/19491034.2015.1004947
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Article ; Online: Linker of nucleoskeleton and cytoskeleton (LINC) complex-mediated actin-dependent nuclear positioning orients centrosomes in migrating myoblasts.

Chang, Wakam / Antoku, Susumu / Östlund, Cecilia / Worman, Howard J / Gundersen, Gregg G

Nucleus (Austin, Tex.)

2015 Volume 6, Issue 1, Page(s) 77–88

Abstract	Myoblast migration is essential for muscle development and repair; however, the factors that contribute to the polarity of migrating myoblasts are relatively unknown. We find that randomly migrating C2C12 myoblasts orient their centrosomes in the direction of migration. Using wounded monolayers, we further show that centrosome orientation is stimulated by the serum factor lysophosphatidic acid (LPA) and involves the rearward movement of the nucleus while the centrosome is maintained at the cell centroid. The rate of nuclear movement correlated with that of actin retrograde flow and both cytochalasin D and blebbistatin prevented nuclear movement and centrosome orientation. Actin-dependent rearward nuclear movement in fibroblasts is mediated by assembly of nuclear membrane nesprin-2G and SUN2 LINC complexes into transmembrane actin-associated nuclear (TAN) lines anchored by A-type lamins and emerin. In C2C12 myoblasts, depletion of nesprin-2G, SUN2 or lamin A/C prevented nuclear movement and endogenous nesprin-2G and a chimeric GFP-mini-nesprin-2G formed TAN lines during nuclear movement. Depleting nesprin-2G strongly interfered with directed cell migration and reduced the efficiency of myoblast fusion into multinucleated myotubes. Our results show that nuclear movement contributes to centrosome orientation and polarity for efficient migration and fusion of myoblasts. Given that mutations in the genes encoding A-type lamins, nesprin-2 and SUN2 cause Emery-Dreifuss muscular dystrophy and related myopathies, our results have implications for understanding the mechanism of disease pathogenesis.
MeSH term(s)	Actins/metabolism ; Animals ; Cell Line ; Cell Movement/drug effects ; Cell Nucleus/drug effects ; Cell Nucleus/metabolism ; Centrosome/drug effects ; Centrosome/metabolism ; Intracellular Signaling Peptides and Proteins/deficiency ; Intracellular Signaling Peptides and Proteins/metabolism ; Lamin Type A/metabolism ; Lysophospholipids/pharmacology ; Membrane Proteins/deficiency ; Membrane Proteins/metabolism ; Mice ; Microfilament Proteins/deficiency ; Microfilament Proteins/metabolism ; Muscle Fibers, Skeletal/cytology ; Myoblasts/cytology ; Myoblasts/drug effects ; Myoblasts/metabolism ; Nerve Tissue Proteins/deficiency ; Nerve Tissue Proteins/metabolism ; Nuclear Proteins/deficiency ; Nuclear Proteins/metabolism
Chemical Substances	Actins ; Intracellular Signaling Peptides and Proteins ; Lamin Type A ; Lysophospholipids ; Membrane Proteins ; Microfilament Proteins ; Nerve Tissue Proteins ; Nuclear Proteins ; SUN2 protein, human ; SYNE2 protein, human ; lamin C ; lysophosphatidic acid (PG6M3969SG)
Language	English
Publishing date	2015
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2619626-8
ISSN	1949-1042 ; 1949-1034
ISSN (online)	1949-1042
ISSN	1949-1034
DOI	10.1080/19491034.2015.1004947
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