• Documents
  • Authors
  • Tables
  • Log in
  • Sign up
  • MetaCart
  • Donate

CiteSeerX logo

Advanced Search Include Citations
Advanced Search Include Citations | Disambiguate

A point mutation in the motor domain of nonmuscle myosin II-B impairs migration of distinct groups of neurons', Mol Biol Cell 15(6 (2004)

by X Ma, S Kawamoto, Y Hara, R S Adelstein
Add To MetaCart

Tools

Sorted by:
Results 1 - 10 of 13
Next 10 →

Loss of cell adhesion causes hydrocephalus in nonmuscle myosin II-B ablated and mutated mice

by Xuefei Ma, Jianjun Bao, Robert S. Adelstein, Paul Forscher , 2007
"... Ablation of nonmuscle myosin (NM) II-B in mice during embryonic development leads to marked enlargement of the cerebral ventricles and destruction of brain tissue, due to hydrocephalus. We have identified a transient mesh-like structure present at the apical border of cells lining the spinal canal o ..."
Abstract - Cited by 5 (0 self) - Add to MetaCart
Ablation of nonmuscle myosin (NM) II-B in mice during embryonic development leads to marked enlargement of the cerebral ventricles and destruction of brain tissue, due to hydrocephalus. We have identified a transient mesh-like structure present at the apical border of cells lining the spinal canal of mice during development. This structure, which only contains the II-B isoform of NM, also contains �-catenin and N-cadherin, consistent with a role in cell adhesion. Ablation of NM II-B or replacement of NM II-B with decreased amounts of a mutant (R709C), motor-impaired NM II-B in mice results in collapse of the mesh-like structure and loss of cell adhesion. This permits the underlying neuroepithelial cells to invade the spinal canal and obstruct cerebral spinal fluid flow. These defects in the CNS of NM II-B–ablated mice seem to be the cause of hydrocephalus. Interestingly, the mesh-like structure and patency of the spinal canal can be restored by increasing expression of the motor-impaired NM II-B, which also rescues hydrocephalus. However, the mutant isoform cannot completely rescue neuronal cell migration. These studies show that the scaffolding properties of NM II-B play an important role in cell adhesion, thereby preventing hydrocephalus during mouse brain development.
(Show Context)

Citation Context

...reviews, see Perez-Figares et al., 2001; Crews et al., 2004). Nonmuscle myosin (NM) II, one of the major cytoskeletal motor proteins, plays an important role in cell migration (Svitkina et al., 1997; =-=Ma et al., 2004-=-; Even-Ram et al., 2007; Vicente-Manzanares et al., 2007), cell–cell adhesion (Conti et al., 2004; Shewan et al., 2005; Giannone et al., 2007), and cell division (De Lozanne and Spudich, 1987; Takeda ...

Myosin IIC: A Third Molecular Motor Driving Neuronal Dynamics

by Steven R. Wylie, Peter D. Chantler , 2007
"... Neuronal dynamics result from the integration of forces developed by molecular motors, especially conventional myosins. Myosin IIC is a recently discovered nonsarcomeric conventional myosin motor, the function of which is poorly understood, particularly in relation to the separate but coupled activi ..."
Abstract - Cited by 2 (0 self) - Add to MetaCart
Neuronal dynamics result from the integration of forces developed by molecular motors, especially conventional myosins. Myosin IIC is a recently discovered nonsarcomeric conventional myosin motor, the function of which is poorly understood, particularly in relation to the separate but coupled activities of its close homologues, myosins IIA and IIB, which participate in neuronal adhesion, outgrowth and retraction. To determine myosin IIC function, we have applied a comparative functional knockdown approach by using isoform-specific antisense oligodeoxyribonucleotides to deplete expression within neuronally derived cells. Myosin IIC was found to be critical for driving neuronal process outgrowth, a function that it shares with myosin IIB. Additionally, myosin IIC modulates neuronal cell adhesion, a function that it shares with myosin IIA but not myosin IIB. Consistent with this role, myosin IIC knockdown caused a concomitant decrease in paxillin-phospho-Tyr118 immunofluorescence, similar to knockdown of myosin IIA but not myosin IIB. Myosin IIC depletion also created a distinctive phenotype with increased cell body diameter, increased vacuolization, and impaired responsiveness to triggered neurite collapse by lysophosphatidic acid. This novel combination of properties suggests that myosin IIC must participate in distinctive cellular roles and reinforces our view that closely related motor isoforms drive diverse functions within neuronal cells.
(Show Context)

Citation Context

...movement and neurite outgrowth (e.g., Kuczmarski and Rosenbaum, 1978; Letourneau, 1981; Miller et al., 1992; Rochlin et al., 1995; Wylie et al., 1998; Bridgman et al., 2001; Chantler and Wylie, 2003; =-=Ma et al., 2004-=-; Even-Ram et al., 2007). The myosin superfamily comprises as many as 24 separate classes of molecule (Foth et al., 2007); yet, many aspects of neuronal movement seem to be dependent on the convention...

unknown title

by Lisa Michelle Kennedy, Lisa M. Kennedy , 2013
"... Genetic analysis of novel regulators of neuronal migration in Caenorhabditis elegans: the insulin/IGF-1 signaling pathway, a chromatin-binding factor ZFP-1 (AF10) and endogenous RNAi ..."
Abstract - Add to MetaCart
Genetic analysis of novel regulators of neuronal migration in Caenorhabditis elegans: the insulin/IGF-1 signaling pathway, a chromatin-binding factor ZFP-1 (AF10) and endogenous RNAi
(Show Context)

Citation Context

...a et al., 2007). Mice that are mutated forsmyosin IIB show abnormal migration of cerebellar granular neurons and abnormal tangentialsmigration of neurons born in the medial ganglionic eminence (MGE) (=-=Ma et al., 2004-=-).sThe microtubule networksThe microtubules play a crucial role in associating the centrosome with the nucleussduring nucleokinesis, as well as in providing stability to the leading process. The micro...

An MYH9 Human Disease Model in Flies: site-directed mutagenesis of the Drosophila nonmuscle myosin II results in hypomorphic alleles with dominant character

by Josef D. Franke, Ruth A. Montague, Wayne L. Rickoll, Daniel P. Kiehart, Daniel P. Kiehart , 2007
"... We investigated whether or not human disease-causing, amino acid substitutions in MYH9 could cause dominant phenotypes when introduced into the sole nonmuscle myosin II heavy chain in Drosophila melanogaster (zip/MyoII). We characterized in vivo the effects of four MYH9-like mutations in the myosin ..."
Abstract - Add to MetaCart
We investigated whether or not human disease-causing, amino acid substitutions in MYH9 could cause dominant phenotypes when introduced into the sole nonmuscle myosin II heavy chain in Drosophila melanogaster (zip/MyoII). We characterized in vivo the effects of four MYH9-like mutations in the myosin rod – R1171C, D1430N, D1847K and R1939X – which occur at highly conserved residues. These engineered mutant heavy chains resulted in D. melanogaster nonmuscle myosin II with partial wild-type function. In a wild-type genetic background, mutant heavy chains were overtly recessive and hypomorphic: each was able to substitute partially for endogenous nonmuscle myosin II heavy chain in animals lacking zygotically produced heavy chain (but the penetrance of rescue was below Mendelian expectation). Moreover, each of the four mutant heavy chains exhibits dominant characteristics when expressed in a sensitized genetic background (flies heterozygous for RhoA mutations). Thus these zip/MyoII MYH9 alleles function, like certain other hypomorphic alleles, as excellent bait in screens for genetic interactors. Our conjecture is that these mutations in D. melanogaster behave comparably to their parent mutations in humans. We further characterized these
(Show Context)

Citation Context

... at Pennsylvania State University on February 20, 2013 effects of knocking-in a mutation analogous to the R702C MYH9-related disorder mutation into the mouse nonmuscle myosin IIB (Myh10; R709C) locus =-=(36, 37)-=-. Heterozygous knock-in mice displayed no observable phenotypes, indicating that this MYH9-like mutation in Myh10 does not act dominantly. Several defects were found in mice homozygous for the R709C m...

1 Function of the Neuron-Specific Alternatively Spliced Isoforms of Nonmuscle Myosin II-B During Mouse Brain Development

by Xuefei Ma, Sachiyo Kawamoto, Jorge Uribe, Robert S. Adelstein, Dr. Robert, S. Adelstein
"... cells, facial neuron migration Abbreviations: NMHC, nonmuscle myosin heavy chain; E, embryonic day; P, postnatal day; ES cell, embryonic stem cell; PBS, phosphate buffered saline; H&E, hematoxylin and eosin; Neo r, neomycin resistance; HMM, heavy meromyosin; CSF, cerebral spinal fluid Correspond ..."
Abstract - Add to MetaCart
cells, facial neuron migration Abbreviations: NMHC, nonmuscle myosin heavy chain; E, embryonic day; P, postnatal day; ES cell, embryonic stem cell; PBS, phosphate buffered saline; H&E, hematoxylin and eosin; Neo r, neomycin resistance; HMM, heavy meromyosin; CSF, cerebral spinal fluid Correspondence should be addressed to:
(Show Context)

Citation Context

...pair of myosin heavy chains along with two pairs of light chains constitute the nonmuscle myosin II molecule and each of these proteins appears to play a role in cell motility (Svitkina et al., 1997; =-=Ma et al., 2004-=-), cell morphology (Wei and Adelstein, 2000), cell adhesion (Conti et al., 2004) and cytokinesis (De Lozanne and Spudich, 1987; Takeda et al., 2003; Bao et al., 2005). Evidence from a number of labora...

1 LOSS OF CELL ADHESION CAUSES HYDROCEPHALUS IN NONMUSCLE MYOSIN II-B ABLATED AND MUTATED MICE

by Xuefei Ma, Jianjun Bao, Robert S. Adelstein, Dr. Xuefei Ma
"... Abbreviations: aPKC, atypical PKC; CSF, cerebral spinal fluid; E, embryonic day; HMM, heavy meromyosin; MLC20, regulatory myosin light chain; NM II, nonmuscle myosin II; NMHC, nonmuscle myosin heavy chain; P, postnatal day. Please address correspondence to: ..."
Abstract - Add to MetaCart
Abbreviations: aPKC, atypical PKC; CSF, cerebral spinal fluid; E, embryonic day; HMM, heavy meromyosin; MLC20, regulatory myosin light chain; NM II, nonmuscle myosin II; NMHC, nonmuscle myosin heavy chain; P, postnatal day. Please address correspondence to:
(Show Context)

Citation Context

...reviews by Crews et al., 2004; PerezFigares et al., 2001). Nonmuscle myosin II (NM II), one of the major cytoskeletal motor proteins, plays an important role in cell migration (Svitkina et al., 1997; =-=Ma et al., 2004-=-, Vicente-Manzanares et al, 2007; Even-Ram et al, 2007), cell-cell adhesion (Conti et al., 2004, Shewan et al., 2005; Giannone et al, 2007), and cell division (De Lozanne and Spudich, 1987; Takeda et ...

unknown title

by Josef D. Franke, Ruth A. Montague, Wayne L. Rickoll, Daniel P. Kiehart , 2007
"... An MYH9 human disease model in flies: site-directed mutagenesis of the Drosophila non-muscle myosin II results in hypomorphic alleles with dominant character ..."
Abstract - Add to MetaCart
An MYH9 human disease model in flies: site-directed mutagenesis of the Drosophila non-muscle myosin II results in hypomorphic alleles with dominant character
(Show Context)

Citation Context

...) was able to poison wildtype myosin-mediated actin filament sliding in vitro. Moreover, the in vivo effect (dominant versus recessive) of these mutations is unknown. Takeda et al. (36) and Ma et al. =-=(37)-=- studied the in vivo effects of knocking-in a mutation analogous to the R702C MYH9-related disorder mutation into the mouse non-muscle myosin IIB (Myh10; R709C) locus. Heterozygous knock-in mice displ...

Function of the Neuron-specific Alternatively Spliced Isoforms of Nonmuscle Myosin II-B during Mouse

by Brain Development, Xuefei Ma, Sachiyo Kawamoto, Jorge Uribe, Robert S. Adelstein , 2005
"... We report that the alternatively spliced isoforms of nonmuscle myosin heavy chain II-B (NHMC II-B) play distinct roles during mouse brain development. The B1-inserted isoform of NMHC II-B, which contains an insert of 10 amino acids near the ATP-binding region (loop 1) of the myosin heavy chain, is i ..."
Abstract - Add to MetaCart
We report that the alternatively spliced isoforms of nonmuscle myosin heavy chain II-B (NHMC II-B) play distinct roles during mouse brain development. The B1-inserted isoform of NMHC II-B, which contains an insert of 10 amino acids near the ATP-binding region (loop 1) of the myosin heavy chain, is involved in normal migration of facial neurons. In contrast, the B2-inserted isoform, which contains an insert of 21 amino acids near the actin-binding region (loop 2), is important for postnatal development of cerebellar Purkinje cells. Deletion of the B1 alternative exon, together with reduced expression of myosin II-B, results in abnormal migration and consequent protrusion of facial neurons into the fourth ventricle. This protrusion is associated with the development of hydrocephalus. Restoring the amount of myosin II-B expression to wild-type levels prevents these defects, showing the importance of total myosin activity in facial neuron migration. In contrast, deletion of the B2 alternative exon results in abnormal development of cerebellar Purkinje cells. Cells lacking the B2-inserted isoform show reduced numbers of dendritic spines and branches. Some of the B2-ablated Purkinje cells are misplaced in the cerebellar molecular layer. All of the B2-ablated mice demonstrated impaired motor coordination.
(Show Context)

Citation Context

... pair of myosin heavy chains along with two pairs of light chains constitute the nonmuscle myosin II molecule, and each of these proteins seems to play a role in cell motility (Svitkina et al., 1997; =-=Ma et al., 2004-=-), cell morphology (Wei and Adelstein, 2000), cell adhesion (Conti et al., 2004), and cytokinesis (De Lozanne and Spudich, 1987; Takeda et al., 2003; Bao et al., 2005). Evidence from a number of labor...

En vue de l’obtention du grade de

by These De Doctorat, Universite Paris, Vi Pierre, Et Marie Curie, Spécialité Neurosciences, Présentée Par, Jean-pierre Baudoin, Pr Jean Mariani, Pr André Goffinet, Directrice De Thèse Remerciements , 2013
"... Sujet de la Thèse: Rôle des microtubules et de l’acto-myosine dans la migration des interneurones corticaux Soutenue le 27 Mars 2008 devant le jury composé de: ..."
Abstract - Add to MetaCart
Sujet de la Thèse: Rôle des microtubules et de l’acto-myosine dans la migration des interneurones corticaux Soutenue le 27 Mars 2008 devant le jury composé de:
(Show Context)

Citation Context

...ur la myosine IIB (vers E16 ; Tullio et al. 2001). Les animaux KO pour la myosine IIB présentent des défauts au niveau du cœur et du cerveau, deux organes riches en cette isoforme (Uren et al. 2000 ; =-=Ma et al. 2004-=-). En particulier une hydrocéphalie sévère se met en place à la fin de la période embryonnaire pour finalement détruire toute la structure cérébrale (Tullio et al. 2001). Cette hydrocéphalie est due v...

JCB: REPORT Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells

by Miguel Vicente-manzanares, Jessica Zareno, Leanna Whitmore, Colin K. Choi, Alan F Horwitz
"... We have used isoform-specifi c RNA interference knockdowns to investigate the roles of myosin IIA (MIIA) and MIIB in the component processes that drive cell migration. Both isoforms reside outside of protrusions and act at a distance to regulate cell protrusion, signaling, and maturation of nascent ..."
Abstract - Add to MetaCart
We have used isoform-specifi c RNA interference knockdowns to investigate the roles of myosin IIA (MIIA) and MIIB in the component processes that drive cell migration. Both isoforms reside outside of protrusions and act at a distance to regulate cell protrusion, signaling, and maturation of nascent adhesions. MIIA also controls the dynamics and size of adhesions in central regions of the cell and contributes to retraction and adhesion disassembly at the rear. In contrast, MIIB establishes front–back polarity and
(Show Context)

Citation Context

...ion, we produced ATPase-inhibited mutants of MIIA and MIIB fused to GFP and mChe. The ATPase activity of N93K-MIIA and R709C-MIIB are inhibited 80 and 75%, respectively, in vitro (Heath et al., 2001; =-=Ma et al., 2004-=-). However, both mutants bind and cross-link, but do not move, actin filaments in vitro (Kim et al., 2005). We used FRAP to show that the mutants exhibit increased time in the actin-bound state, as ex...

Powered by: Apache Solr
  • About CiteSeerX
  • Submit and Index Documents
  • Privacy Policy
  • Help
  • Data
  • Source
  • Contact Us

Developed at and hosted by The College of Information Sciences and Technology

© 2007-2016 The Pennsylvania State University