scholarly journals Diverse functions of myosin VI in spermiogenesis

2021 ◽  
Author(s):  
Przemysław Zakrzewski ◽  
Marta Lenartowska ◽  
Folma Buss
Keyword(s):  
Adaptor Proteins ◽  
Actin Dynamics ◽  
Actin Binding ◽  
Animal Cells ◽  
C Elegans ◽  
Cellular Processes ◽  
Sperm Development ◽  
Membrane Compartments ◽  
Myosin Motors ◽  
The Many

AbstractSpermiogenesis is the final stage of spermatogenesis, a differentiation process during which unpolarized spermatids undergo excessive remodeling that results in the formation of sperm. The actin cytoskeleton and associated actin-binding proteins play crucial roles during this process regulating organelle or vesicle delivery/segregation and forming unique testicular structures involved in spermatid remodeling. In addition, several myosin motor proteins including MYO6 generate force and movement during sperm differentiation. MYO6 is highly unusual as it moves towards the minus end of actin filaments in the opposite direction to other myosin motors. This specialized feature of MYO6 may explain the many proposed functions of this myosin in a wide array of cellular processes in animal cells, including endocytosis, secretion, stabilization of the Golgi complex, and regulation of actin dynamics. These diverse roles of MYO6 are mediated by a range of specialized cargo-adaptor proteins that link this myosin to distinct cellular compartments and processes. During sperm development in a number of different organisms, MYO6 carries out pivotal functions. In Drosophila, the MYO6 ortholog regulates actin reorganization during spermatid individualization and male KO flies are sterile. In C. elegans, the MYO6 ortholog mediates asymmetric segregation of cytosolic material and spermatid budding through cytokinesis, whereas in mice, this myosin regulates assembly of highly specialized actin-rich structures and formation of membrane compartments to allow the formation of fully differentiated sperm. In this review, we will present an overview and compare the diverse function of MYO6 in the specialized adaptations of spermiogenesis in flies, worms, and mammals.

scholarly journals Myosin 1b is an actin depolymerase

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Julien Pernier ◽  
Remy Kusters ◽  
Hugo Bousquet ◽  
Thibaut Lagny ◽  
Antoine Morchain ◽  
...  
Keyword(s):  
Myosin Ii ◽  
Actin Dynamics ◽  
Myosin Motor ◽  
Actin Depolymerization ◽  
Cellular Processes ◽  
Myosin Motors ◽  
Singular Interactions ◽  
Sliding Motility

AbstractThe regulation of actin dynamics is essential for various cellular processes. Former evidence suggests a correlation between the function of non-conventional myosin motors and actin dynamics. Here we investigate the contribution of myosin 1b to actin dynamics using sliding motility assays. We observe that sliding on myosin 1b immobilized or bound to a fluid bilayer enhances actin depolymerization at the barbed end, while sliding on myosin II, although 5 times faster, has no effect. This work reveals a non-conventional myosin motor as another type of depolymerase and points to its singular interactions with the actin barbed end.

scholarly journals Inhibition of platelet function by targeting the platelet cytoskeleton via the LIMK-signaling pathway

2018 ◽  
Author(s):  
Juliana Antonipillai ◽  
Sheena Rigby ◽  
Nicole Bassler ◽  
Karlheinz Peter ◽  
Ora Bernard
Keyword(s):  
Platelet Function ◽  
Actin Dynamics ◽  
Actin Binding ◽  
Lim Kinase ◽  
Cellular Processes ◽  
New Strategy ◽  
Platelet Aggregates ◽  
Dynamic Structures ◽  
Shape Changes ◽  
Platelet Shape

AbstractActin is highly abundant in platelets, and platelet function is dependent on actin structures. Actin filaments are dynamic structures involved in many cellular processes including platelet shape changes and adhesion. The actin cytoskeleton is tightly regulated by actin-binding proteins, which include the members of the actin depolymerising factor (ADF)/cofilin family. LIM kinase (LIMK) and slingshot phosphatase (SSH-1L) regulate actin dynamics by controlling the binding affinity of ADF/cofilin towards actin. We hypothesised that inhibition of LIMK activity may prevent the changes in platelet shape during their activation and therefore their function by controlling the dynamics of Factin. Therefore, inhibition of LIMK activity may represent an attractive new strategy to control and inhibit platelet function; particularly the formation of stable platelet aggregates and thus stable thrombi.

scholarly journals Structure of the actin-depolymerizing factor homology domain in complex with actin

2008 ◽  
Vol 182 (1) ◽  
pp. 51-59 ◽  
Author(s):  
Ville O. Paavilainen ◽  
Esko Oksanen ◽  
Adrian Goldman ◽  
Pekka Lappalainen
Keyword(s):  
Crystal Structure ◽  
Atomic Structure ◽  
Actin Filaments ◽  
Driving Force ◽  
Actin Dynamics ◽  
Actin Binding ◽  
Actin Monomer ◽  
Nucleotide Exchange ◽  
Actin Depolymerizing Factor ◽  
Cellular Processes

Actin dynamics provide the driving force for many cellular processes including motility and endocytosis. Among the central cytoskeletal regulators are actin-depolymerizing factor (ADF)/cofilin, which depolymerizes actin filaments, and twinfilin, which sequesters actin monomers and caps filament barbed ends. Both interact with actin through an ADF homology (ADF-H) domain, which is also found in several other actin-binding proteins. However, in the absence of an atomic structure for the ADF-H domain in complex with actin, the mechanism by which these proteins interact with actin has remained unknown. Here, we present the crystal structure of twinfilin's C-terminal ADF-H domain in complex with an actin monomer. This domain binds between actin subdomains 1 and 3 through an interface that is conserved among ADF-H domain proteins. Based on this structure, we suggest a mechanism by which ADF/cofilin and twinfilin inhibit nucleotide exchange of actin monomers and present a model for how ADF/cofilin induces filament depolymerization by weakening intrafilament interactions.

scholarly journals Critical Roles of Phosphorylation and Actin Binding Motifs, but Not the Central Proline-rich Region, for Ena/Vasodilator-stimulated Phosphoprotein (VASP) Function during Cell Migration

2002 ◽  
Vol 13 (7) ◽  
pp. 2533-2546 ◽  
Author(s):  
Joseph J. Loureiro ◽  
Douglas A. Rubinson ◽  
James E. Bear ◽  
Gretchen A. Baltus ◽  
Adam V. Kwiatkowski ◽  
...  
Keyword(s):  
Cell Motility ◽  
Cell Movement ◽  
Protein Family ◽  
Actin Dynamics ◽  
Actin Binding ◽  
Binding Motif ◽  
Conserved Sequence ◽  
Cellular Processes ◽  
Sequence Elements

The Ena/vasodilator-stimulated phosphoprotein (VASP) protein family is implicated in the regulation of a number of actin-based cellular processes, including lamellipodial protrusion necessary for whole cell translocation. A growing body of evidence derived largely from in vitro biochemical experiments using purified proteins, cell-free extracts, and pathogen motility has begun to suggest various mechanistic roles for Ena/VASP proteins in the control of actin dynamics. Using complementation of phenotypes in Ena/VASP-deficient cells and overexpression in normal fibroblasts, we have assayed the function of a panel of mutants in one member of this family, Mena, by mutating highly conserved sequence elements found in this protein family. Surprisingly, deletion of sites required for binding of the actin monomer-binding protein profilin, a known ligand of Ena/VASP proteins, has no effect on the ability of Mena to regulate random cell motility. Our analysis revealed two features essential for Ena/VASP function in cell movement, cyclic nucleotide-dependent kinase phosphorylation sites and an F-actin binding motif. Interestingly, expression of the C-terminal EVH2 domain alone is sufficient to complement loss of Ena/VASP function in random cell motility.

scholarly journals Roles of Actin in the Morphogenesis of the Early Caenorhabditis elegans Embryo

2020 ◽  
Vol 21 (10) ◽  
pp. 3652
Author(s):  
Dureen Samandar Eweis ◽  
Julie Plastino
Keyword(s):  
Cell Division ◽  
Caenorhabditis Elegans ◽  
Asymmetric Cell Division ◽  
Cell Types ◽  
Actin Dynamics ◽  
Actin Binding ◽  
Asymmetric Cell Divisions ◽  
C Elegans ◽  
Asymmetric Divisions ◽  
Different Cell Types

The cell shape changes that ensure asymmetric cell divisions are crucial for correct development, as asymmetric divisions allow for the formation of different cell types and therefore different tissues. The first division of the Caenorhabditis elegans embryo has emerged as a powerful model for understanding asymmetric cell division. The dynamics of microtubules, polarity proteins, and the actin cytoskeleton are all key for this process. In this review, we highlight studies from the last five years revealing new insights about the role of actin dynamics in the first asymmetric cell division of the early C. elegans embryo. Recent results concerning the roles of actin and actin binding proteins in symmetry breaking, cortical flows, cortical integrity, and cleavage furrow formation are described.

scholarly journals Plastin 3 in health and disease: a matter of balance

2021 ◽  
Author(s):  
Lisa Wolff ◽  
Eike A. Strathmann ◽  
Ilka Müller ◽  
Daniela Mählich ◽  
Charlotte Veltman ◽  
...  
Keyword(s):  
Bone Fractures ◽  
Muscular Atrophy ◽  
X Inactivation ◽  
Actin Dynamics ◽  
Actin Binding ◽  
Specific Expression ◽  
Expression Variability ◽  
Cellular Processes ◽  
Long Time ◽  
Health And Disease

AbstractFor a long time, PLS3 (plastin 3, also known as T-plastin or fimbrin) has been considered a rather inconspicuous protein, involved in F-actin-binding and -bundling. However, in recent years, a plethora of discoveries have turned PLS3 into a highly interesting protein involved in many cellular processes, signaling pathways, and diseases. PLS3 is localized on the X-chromosome, but shows sex-specific, inter-individual and tissue-specific expression variability pointing towards skewed X-inactivation. PLS3 is expressed in all solid tissues but usually not in hematopoietic cells. When escaping X-inactivation, PLS3 triggers a plethora of different types of cancers. Elevated PLS3 levels are considered a prognostic biomarker for cancer and refractory response to therapies. When it is knocked out or mutated in humans and mice, it causes osteoporosis with bone fractures; it is the only protein involved in actin dynamics responsible for osteoporosis. Instead, when PLS3 is upregulated, it acts as a highly protective SMN-independent modifier in spinal muscular atrophy (SMA). Here, it seems to counteract reduced F-actin levels by restoring impaired endocytosis and disturbed calcium homeostasis caused by reduced SMN levels. In contrast, an upregulation of PLS3 on wild-type level might cause osteoarthritis. This emphasizes that the amount of PLS3 in our cells must be precisely balanced; both too much and too little can be detrimental. Actin-dynamics, regulated by PLS3 among others, are crucial in a lot of cellular processes including endocytosis, cell migration, axonal growth, neurotransmission, translation, and others. Also, PLS3 levels influence the infection with different bacteria, mycosis, and other pathogens.

scholarly journals A new actin depolymerase: a Myosin 1 motor

2018 ◽  
Author(s):  
Julien Pernier ◽  
Remy Kusters ◽  
Hugo Bousquet ◽  
Thibaut Lagny ◽  
Antoine Morchain ◽  
...  
Keyword(s):  
Myosin Ii ◽  
Actin Dynamics ◽  
Myosin Motor ◽  
Actin Depolymerization ◽  
Cellular Processes ◽  
New Type ◽  
Myosin Motors ◽  
Singular Interactions ◽  
Sliding Motility

AbstractThe regulation of actin dynamics is essential for various cellular processes. Former evidence suggests a correlation between the function of non-conventional myosin motors and actin dynamics. We investigate the contribution of myosin1b to actin dynamics using sliding motility assays. We observe that sliding on myosin1b immobilized or bound to a fluid bilayer enhances actin depolymerization at the barbed end, while sliding on myosin II, although 5 times faster, has no effect. This work reveals a non-conventional myosin motor as a new type of depolymerase and points to its singular interactions with the actin barbed end.

scholarly journals Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules

2011 ◽  
Vol 22 (23) ◽  
pp. 4575-4587 ◽  
Author(s):  
Jeremie Gaillard ◽  
Vinay Ramabhadran ◽  
Emmanuelle Neumanne ◽  
Pinar Gurel ◽  
Laurent Blanchoin ◽  
...  
Keyword(s):  
Actin Filaments ◽  
Actin Polymerization ◽  
Actin Dynamics ◽  
Actin Binding ◽  
Differential Function ◽  
Cellular Processes ◽  
High Affinity ◽  
C Terminus ◽  
Molecular Machinery ◽  
Cytoskeletal Elements

A number of cellular processes use both microtubules and actin filaments, but the molecular machinery linking these two cytoskeletal elements remains to be elucidated in detail. Formins are actin-binding proteins that have multiple effects on actin dynamics, and one formin, mDia2, has been shown to bind and stabilize microtubules through its formin homology 2 (FH2) domain. Here we show that three formins, INF2, mDia1, and mDia2, display important differences in their interactions with microtubules and actin. Constructs containing FH1, FH2, and C-terminal domains of all three formins bind microtubules with high affinity (Kd < 100 nM). However, only mDia2 binds microtubules at 1:1 stoichiometry, with INF2 and mDia1 showing saturating binding at approximately 1:3 (formin dimer:tubulin dimer). INF2-FH1FH2C is a potent microtubule-bundling protein, an effect that results in a large reduction in catastrophe rate. In contrast, neither mDia1 nor mDia2 is a potent microtubule bundler. The C-termini of mDia2 and INF2 have different functions in microtubule interaction, with mDia2's C-terminus required for high-affinity binding and INF2's C-terminus required for bundling. mDia2's C-terminus directly binds microtubules with submicromolar affinity. These formins also differ in their abilities to bind actin and microtubules simultaneously. Microtubules strongly inhibit actin polymerization by mDia2, whereas they moderately inhibit mDia1 and have no effect on INF2. Conversely, actin monomers inhibit microtubule binding/bundling by INF2 but do not affect mDia1 or mDia2. These differences in interactions with microtubules and actin suggest differential function in cellular processes requiring both cytoskeletal elements.

scholarly journals Magnaporthe oryzae Abp1, a MoArk1 Kinase-Interacting Actin Binding Protein, Links Actin Cytoskeleton Regulation to Growth, Endocytosis, and Pathogenesis

2019 ◽  
Vol 32 (4) ◽  
pp. 437-451 ◽  
Author(s):  
Lianwei Li ◽  
Shengpei Zhang ◽  
Xinyu Liu ◽  
Rui Yu ◽  
Xinrui Li ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Magnaporthe Oryzae ◽  
Binding Protein ◽  
Normal Growth ◽  
Underlying Mechanism ◽  
Actin Dynamics ◽  
Actin Binding ◽  
Actin Binding Protein ◽  
Cellular Processes ◽  
Blast Fungus

The actin cytoskeleton and actin-coupled endocytosis are conserved cellular processes required for the normal growth and pathogenesis of the rice blast fungus Magnaporthe oryzae. We have previously shown that actin regulating kinase MoArk1 regulates actin dynamics and endocytosis to play a key role in virulence of the fungus. To understand the underlying mechanism, we have characterized the actin-binding protein MoAbp1 that interacts with MoArk1 from M. oryzae. The ΔMoabp1 mutant exhibited delayed endocytosis and defects in growth, host penetration, and invasive growth. Consistent with its putative function associated with actin-binding, MoAbp1 regulates the localization of actin patches and plays a role in MoArk1 phosphorylation. In addition, MoAbp1 interacts with MoCap (adenylyl cyclase–associated protein) affecting its normal patch localization pattern and the actin protein MoAct1 through its conserved domains. Taken together, our results support a notion that MoAbp1 functions as a protein scaffold linking MoArk1, MoCap1, and MoAct1 to regulate actin cytoskeleton dynamics critical in growth and pathogenicity of the blast fungus.

scholarly journals The Amazing Acrobat: Yeast’s Histone H3K56 Juggles Several Important Roles While Maintaining Perfect Balance

Genes ◽  
2021 ◽  
Vol 12 (3) ◽  
pp. 342
Author(s):  
Lihi Gershon ◽  
Martin Kupiec
Keyword(s):  
Dna Replication ◽  
Genome Stability ◽  
Entry And Exit ◽  
Yeast Saccharomyces Cerevisiae ◽  
Cellular Processes ◽  
M Phase ◽  
Dna Replication And Repair ◽  
H3k56 Acetylation ◽  
Timely Fashion ◽  
The Many

Acetylation on lysine 56 of histone H3 of the yeast Saccharomyces cerevisiae has been implicated in many cellular processes that affect genome stability. Despite being the object of much research, the complete scope of the roles played by K56 acetylation is not fully understood even today. The acetylation is put in place at the S-phase of the cell cycle, in order to flag newly synthesized histones that are incorporated during DNA replication. The signal is removed by two redundant deacetylases, Hst3 and Hst4, at the entry to G2/M phase. Its crucial location, at the entry and exit points of the DNA into and out of the nucleosome, makes this a central modification, and dictates that if acetylation and deacetylation are not well concerted and executed in a timely fashion, severe genomic instability arises. In this review, we explore the wealth of information available on the many roles played by H3K56 acetylation and the deacetylases Hst3 and Hst4 in DNA replication and repair.

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