Localization of myosin II A and B isoforms in cultured neurons

M.W. Rochlin; K. Itoh; R.S. Adelstein; P.C. Bridgman

Summary

Tension generated by growth cones regulates both the rate and the direction of neurite growth. The most likely effectors of tension generation are actin and myosins. We are investigating the role of conventional myosin in growth cone advance. In this paper we report the localization of the two most prominent isoforms of brain myosin II in growth cones, neurites and cell bodies of rat superior cervical ganglion neurons. Affinity purified polyclonal antibodies were prepared against unique peptide sequences from human and rat A and B isoforms of myosin heavy chain. Although each of these antibodies brightly stained nonneuronal cells, antibodies to myosin heavy chain B stained neurons with greater intensity than antibodies to myosin heavy chain A. In growth cones, myosin heavy chain B was most concentrated in the margin bordering the thickened, organelle-rich central region and the thin, actin-rich peripheral region. The staining colocalized with actin bundles proximal and distal to the marginal zone, though the staining was more prominent proximally. The trailing edge of growth cones and the distal portion of the neurite often had a rimmed appearance, but more proximal regions of neurites had cytoplasmic labelling. Localizing MHC-B in growth cones previously monitored during advance (using differential interference contrast microscopy) revealed a positive correlation with edges at which retraction had just occurred and a negative correlation with lamellipodia that had recently undergone protrusion. Cell bodies were brightly labelled for myosin heavy chain B. Myosin heavy chain A staining was dimmer and its colocalization with filamentous actin bundles in growth cones was less striking than that of myosin heavy chain B. Growth cones stained for both myosin heavy chain A and B revealed that the two antigens overlapped frequently, but not exclusively, and that myosin heavy chain A lacked the elevation in the marginal zone that was characteristic of myosin heavy chain B. The pattern of staining we observed is consistent with a prominent role for myosin heavy chain B in either generating tension between widely separated areas of the growth cone, or bundling of actin filaments, which would enable other motors to effect this tension. These data support the notion that conventional myosin is important in growth cone advance and turning.

REFERENCES

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2. Block S. M.
(1984). A miniature flow cell designed for rapid exchange of media under high-power microscope objective. J. Gen. Microbiol 130, 2915–2920
OpenUrl Abstract/FREE Full Text
1. Bridgman P. C. and
2. Dailey M. E.
(1989). The organization of myosin and actin in rapid frozen nerve growth cones. J. Cell Biol 108, 95–109
OpenUrl Abstract/FREE Full Text
1. Burridge K. and
2. Bray D.
(1975). Purification and structural analysis of myosins from brain and other non-muscle tissues. J. Mol. Biol 99, 1–14
OpenUrl CrossRef PubMed Web of Science
1. Cheney R. E.,
2. O'Shea M. K.,
3. Heuser J. E.,
4. Coelho M. V.,
5. Wolenski J. S.,
6. Espreafico E. M.,
7. Forscher P.,
8. Larson R. E. and
9. Mooseker M. S.
(1993). Brain myosin-V is a two-headed unconventional myosin with motor activity. Cell 75, 13–23
OpenUrl CrossRef PubMed Web of Science
1. Cheng T. P. O.,
2. Murakami N. and
3. Elzinga M.
(1992). Localization of myosin-IIB at the leading-edge of growth cones from rat dorsal-root ganglionic cells. FEBS Lett 311, 91–94
OpenUrl CrossRef PubMed Web of Science
1. De Lozanne A. and
2. Spudich J. A.
(1987). Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science 236, 1086–1091
OpenUrl Abstract/FREE Full Text
1. Espreafico E. M.,
2. Cheney R. E.,
3. Matteoli M.,
4. Nascimento A. A. C.,
5. De Camilli P. V.,
6. Larson R. E. and
7. Mooseker M. S.
(1992). Primary structure and cellular localization of chicken brain myosin-V (pl90), an unconventional myosin with calmodulin light chains. J. Cell Biol 119, 1541–1557
OpenUrl Abstract/FREE Full Text
1. Fath K. and
2. Burgess D. R.
(1993). Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically-oriented peripheral membrane protein. J. Cell Biol 120, 117–27
OpenUrl Abstract/FREE Full Text
1. Forscher P. and
2. Smith S. J.
(1988). Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone. J. Cell Biol 107, 1505–1516
OpenUrl Abstract/FREE Full Text
1. Honer B.,
2. Citi S.,
3. Kendrick-Jones J. and
4. Jockusch B. M.
(1988). Modulation of cellular morphology and locomotory activity by antibodies against myosin. J. Cell Biol 107, 2181–2189
OpenUrl Abstract/FREE Full Text
1. Itoh K. and
2. Adelstein R. S.
(1995). Neuronal cell expression of inserted isoforms of vertebrate nonmuscle myosin heavy chain II-B. J. Biol. Chem 270, 14533–14540
OpenUrl Abstract/FREE Full Text
1. Jay P. Y.,
2. Pham P. A.,
3. Wong S. A. and
4. Elson E. L.
(1995). A mechanical function of myosin II in cell motility. J. Cell Sci 108, 387–393
OpenUrl Abstract/FREE Full Text
1. Johnston G. C.,
2. Prendergast J. A. and
3. Singer R. A.
(1991). The saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectoral transport of vesicles. J. Cell Biol 113, 539–551
OpenUrl Abstract/FREE Full Text
1. Kawamoto S. and
2. Adelstein R. S.
(1991). Chicken nonmuscle myosin heavy chains: differential expression of two mRNAs and evidence for two different polypeptides. J. Cell Biol 112, 915–924
OpenUrl Abstract/FREE Full Text
1. Knecht D. A. and
2. Loomis W. F.
(1987). Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium. Science 236, 1081–1086
OpenUrl Abstract/FREE Full Text
1. Lamoureux P.,
2. Buxbaum R. E. and
3. Heidemann S. R.
(1989). Direct evidence that growth cones pull. Nature 340, 159–162
OpenUrl CrossRef PubMed
1. Lee J.,
2. Leonard M.,
3. Oliver T.,
4. Ishihara A. and
5. Jacobson K.
(1994). Traction forces generated by locomoting keratocytes. J. Cell Biol 127, 1957–1964
OpenUrl Abstract/FREE Full Text
1. Lewis A. K. and
2. Bridgman P. C.
(1992). Nerve growth cone lamellipodia contain two populations of actin filaments that differ in organization and polarity. J. Cell Biol 119, 1219–1243
OpenUrl Abstract/FREE Full Text
1. Mabuchi I. and
2. Okuno M.
(1977). The effect of myosin antibody on the division of starfish blastomeres. J. Cell Biol 74, 251–263
OpenUrl Abstract/FREE Full Text
1. Maupin P.,
2. Phillips C. L.,
3. Adelstein R. S. and
4. Pollard T. D.
(1994). Differential localization of myosin-II isozymes in human cultured cells and blood cells. J. Cell Sci 107, 3077–3090
OpenUrl Abstract/FREE Full Text
1. McKenna N. M.,
2. Wang Y. and
3. Konkel M. E.
(1989). Formation and movement of myosin-containing structures in living fibroblasts. J. Cell Biol 109, 1163–1172
OpenUrl Abstract/FREE Full Text
1. Miller M.,
2. Bower E.,
3. Levitt P.,
4. Li D. and
5. Chantler P. D.
(1992). Myosin II distribution in neurons is consistent with a role in growth cone motility but not synaptic vesicle mobilization. Neuron 8, 25–44
OpenUrl CrossRef PubMed Web of Science
1. Murakami N.,
2. Mehta P. and
3. Elzinga M.
(1991). Studies on the distribution of cellular myosin with antibodies to isoform-specific synthetic peptides. FEBS Lett 278, 23–25
OpenUrl CrossRef PubMed Web of Science
1. Murakami N. and
2. Elzinga M.
(1992). Immunohistochemical studies on the distribution of cellular myosin II isoforms in brain and aorta. Cell Motil. Cytoskel 22, 281–295
OpenUrl CrossRef PubMed Web of Science
1. Phillips C. L.,
2. Yamakawa K. and
3. Adelstein R. S.
(1995). Cloning of the cDNA encoding human nonmuscle myosin heavy chain B and analysis of human tissues with isoform-specific antibodies. J. Muscle Res. Cell Motil 16, 379–389
OpenUrl CrossRef PubMed Web of Science
1. Ruppert C.,
2. Kroschewski R. and
3. Bahler M.
(1993). Identification, characterization and cloning of myr 1, a mammalian myosin I. J. Cell Biol 120, 1393–1403
OpenUrl Abstract/FREE Full Text
1. Saez C. G.,
2. Myers J. C.,
3. Shows T. B. and
4. Leinwand L. A.
(1990). Human nonmuscle myosin heavy chain mRNA: Generation of diversity through alternative polyadenylation. Proc. Nat. Acad. Sci. USA 87, 1164–1168
OpenUrl Abstract/FREE Full Text
1. Simons M.,
2. Wang M.,
3. McBride O. W.,
4. Kawamoto S.,
5. Yamakawa K.,
6. Gdula D.,
7. Adelstein R. S. and
8. Weir L.
(1991). Human nonmuscle myosin heavy chains are encoded by two genes located on different chromosomes. Circul. Res 69, 530–539
OpenUrl Abstract/FREE Full Text
1. Small J. V.
(1994). Microfilament-based motility in non-muscle cells. Curr. Opin. Cell Biol 1, 75–79
OpenUrl
1. Strobel M. C.,
2. Seperack P. K.,
3. Copeland N. G. and
4. Jenkins N. A.
(1990). Molecular analysis of two mouse dilute locus deletion mutations: spontaneous dilute lethal205and radiation-induced dilute prenatal lethal Aa2 alleles. Mol. Cell Biol 10, 501–509
OpenUrl Abstract/FREE Full Text
1. Sun W. and
2. Chantler P. D.
(1991). A unique cellular myosin II exhibiting differential expression in the cerebral cortex. Biochem. Biophys. Res. Commun 175, 244–249
OpenUrl CrossRef PubMed
1. Warrick H. M. and
2. Spudich J. A.
(1987). Myosin structure and function in cell motility. Annu. Rev. Cell Biol 3, 379–421
OpenUrl CrossRef Web of Science
1. Waterston R. H.
(1989). The minor myosin heavy chain, mhcA, of Caenorhabditis elegans is necessary for the initiation of thick filament assembly. EMBO J 8, 3429–3436
OpenUrl PubMed Web of Science
1. Zot H. G.,
2. Doberstein S. K. and
3. Pollard T. D.
(1992). Myosin-I moves actin filaments on a phospholipid substrate: implications for membrane targeting. J. Cell Biol 116, 367–376
OpenUrl Abstract/FREE Full Text

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[1] Berg H. C. and
Block S. M.
(1984). A miniature flow cell designed for rapid exchange of media under high-power microscope objective. J. Gen. Microbiol 130, 2915–2920
OpenUrl Abstract/FREE Full Text

[2] Berg H. C. and

[3] Block S. M.

[4] Bridgman P. C. and
Dailey M. E.
(1989). The organization of myosin and actin in rapid frozen nerve growth cones. J. Cell Biol 108, 95–109
OpenUrl Abstract/FREE Full Text

[5] Bridgman P. C. and

[6] Dailey M. E.

[7] Burridge K. and
Bray D.
(1975). Purification and structural analysis of myosins from brain and other non-muscle tissues. J. Mol. Biol 99, 1–14
OpenUrl CrossRef PubMed Web of Science

[8] Burridge K. and

[9] Bray D.

[10] Cheney R. E.,
O'Shea M. K.,
Heuser J. E.,
Coelho M. V.,
Wolenski J. S.,
Espreafico E. M.,
Forscher P.,
Larson R. E. and
Mooseker M. S.
(1993). Brain myosin-V is a two-headed unconventional myosin with motor activity. Cell 75, 13–23
OpenUrl CrossRef PubMed Web of Science

[11] Cheney R. E.,

[12] O'Shea M. K.,

[13] Heuser J. E.,

[14] Coelho M. V.,

[15] Wolenski J. S.,

[16] Espreafico E. M.,

[17] Forscher P.,

[18] Larson R. E. and

[19] Mooseker M. S.

[20] Cheng T. P. O.,
Murakami N. and
Elzinga M.
(1992). Localization of myosin-IIB at the leading-edge of growth cones from rat dorsal-root ganglionic cells. FEBS Lett 311, 91–94
OpenUrl CrossRef PubMed Web of Science

[21] Cheng T. P. O.,

[22] Murakami N. and

[23] Elzinga M.

[24] De Lozanne A. and
Spudich J. A.
(1987). Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science 236, 1086–1091
OpenUrl Abstract/FREE Full Text

[25] De Lozanne A. and

[26] Spudich J. A.

[27] Espreafico E. M.,
Cheney R. E.,
Matteoli M.,
Nascimento A. A. C.,
De Camilli P. V.,
Larson R. E. and
Mooseker M. S.
(1992). Primary structure and cellular localization of chicken brain myosin-V (pl90), an unconventional myosin with calmodulin light chains. J. Cell Biol 119, 1541–1557
OpenUrl Abstract/FREE Full Text

[28] Espreafico E. M.,

[29] Cheney R. E.,

[30] Matteoli M.,

[31] Nascimento A. A. C.,

[32] De Camilli P. V.,

[33] Larson R. E. and

[34] Mooseker M. S.

[35] Fath K. and
Burgess D. R.
(1993). Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically-oriented peripheral membrane protein. J. Cell Biol 120, 117–27
OpenUrl Abstract/FREE Full Text

[36] Fath K. and

[37] Burgess D. R.

[38] Forscher P. and
Smith S. J.
(1988). Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone. J. Cell Biol 107, 1505–1516
OpenUrl Abstract/FREE Full Text

[39] Forscher P. and

[40] Smith S. J.

[41] Honer B.,
Citi S.,
Kendrick-Jones J. and
Jockusch B. M.
(1988). Modulation of cellular morphology and locomotory activity by antibodies against myosin. J. Cell Biol 107, 2181–2189
OpenUrl Abstract/FREE Full Text

[42] Honer B.,

[43] Citi S.,

[44] Kendrick-Jones J. and

[45] Jockusch B. M.

[46] Itoh K. and
Adelstein R. S.
(1995). Neuronal cell expression of inserted isoforms of vertebrate nonmuscle myosin heavy chain II-B. J. Biol. Chem 270, 14533–14540
OpenUrl Abstract/FREE Full Text

[47] Itoh K. and

[48] Adelstein R. S.

[49] Jay P. Y.,
Pham P. A.,
Wong S. A. and
Elson E. L.
(1995). A mechanical function of myosin II in cell motility. J. Cell Sci 108, 387–393
OpenUrl Abstract/FREE Full Text

[50] Jay P. Y.,

[51] Pham P. A.,

[52] Wong S. A. and

[53] Elson E. L.

[54] Johnston G. C.,
Prendergast J. A. and
Singer R. A.
(1991). The saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectoral transport of vesicles. J. Cell Biol 113, 539–551
OpenUrl Abstract/FREE Full Text

[55] Johnston G. C.,

[56] Prendergast J. A. and

[57] Singer R. A.

[58] Kawamoto S. and
Adelstein R. S.
(1991). Chicken nonmuscle myosin heavy chains: differential expression of two mRNAs and evidence for two different polypeptides. J. Cell Biol 112, 915–924
OpenUrl Abstract/FREE Full Text

[59] Kawamoto S. and

[60] Adelstein R. S.

[61] Knecht D. A. and
Loomis W. F.
(1987). Antisense RNA inactivation of myosin heavy chain gene expression in Dictyostelium. Science 236, 1081–1086
OpenUrl Abstract/FREE Full Text

[62] Knecht D. A. and

[63] Loomis W. F.

[64] Lamoureux P.,
Buxbaum R. E. and
Heidemann S. R.
(1989). Direct evidence that growth cones pull. Nature 340, 159–162
OpenUrl CrossRef PubMed

[65] Lamoureux P.,

[66] Buxbaum R. E. and

[67] Heidemann S. R.

[68] Lee J.,
Leonard M.,
Oliver T.,
Ishihara A. and
Jacobson K.
(1994). Traction forces generated by locomoting keratocytes. J. Cell Biol 127, 1957–1964
OpenUrl Abstract/FREE Full Text

[69] Lee J.,

[70] Leonard M.,

[71] Oliver T.,

[72] Ishihara A. and

[73] Jacobson K.

[74] Lewis A. K. and
Bridgman P. C.
(1992). Nerve growth cone lamellipodia contain two populations of actin filaments that differ in organization and polarity. J. Cell Biol 119, 1219–1243
OpenUrl Abstract/FREE Full Text

[75] Lewis A. K. and

[76] Bridgman P. C.

[77] Mabuchi I. and
Okuno M.
(1977). The effect of myosin antibody on the division of starfish blastomeres. J. Cell Biol 74, 251–263
OpenUrl Abstract/FREE Full Text

[78] Mabuchi I. and

[79] Okuno M.

[80] Maupin P.,
Phillips C. L.,
Adelstein R. S. and
Pollard T. D.
(1994). Differential localization of myosin-II isozymes in human cultured cells and blood cells. J. Cell Sci 107, 3077–3090
OpenUrl Abstract/FREE Full Text

[81] Maupin P.,

[82] Phillips C. L.,

[83] Adelstein R. S. and

[84] Pollard T. D.

[85] McKenna N. M.,
Wang Y. and
Konkel M. E.
(1989). Formation and movement of myosin-containing structures in living fibroblasts. J. Cell Biol 109, 1163–1172
OpenUrl Abstract/FREE Full Text

[86] McKenna N. M.,

[87] Wang Y. and

[88] Konkel M. E.

[89] Miller M.,
Bower E.,
Levitt P.,
Li D. and
Chantler P. D.
(1992). Myosin II distribution in neurons is consistent with a role in growth cone motility but not synaptic vesicle mobilization. Neuron 8, 25–44
OpenUrl CrossRef PubMed Web of Science

[90] Miller M.,

[91] Bower E.,

[92] Levitt P.,

[93] Li D. and

[94] Chantler P. D.

[95] Murakami N.,
Mehta P. and
Elzinga M.
(1991). Studies on the distribution of cellular myosin with antibodies to isoform-specific synthetic peptides. FEBS Lett 278, 23–25
OpenUrl CrossRef PubMed Web of Science

[96] Murakami N.,

[97] Mehta P. and

[98] Elzinga M.

[99] Murakami N. and
Elzinga M.
(1992). Immunohistochemical studies on the distribution of cellular myosin II isoforms in brain and aorta. Cell Motil. Cytoskel 22, 281–295
OpenUrl CrossRef PubMed Web of Science

[100] Murakami N. and

[101] Elzinga M.

[102] Phillips C. L.,
Yamakawa K. and
Adelstein R. S.
(1995). Cloning of the cDNA encoding human nonmuscle myosin heavy chain B and analysis of human tissues with isoform-specific antibodies. J. Muscle Res. Cell Motil 16, 379–389
OpenUrl CrossRef PubMed Web of Science

[103] Phillips C. L.,

[104] Yamakawa K. and

[105] Adelstein R. S.

[106] Ruppert C.,
Kroschewski R. and
Bahler M.
(1993). Identification, characterization and cloning of myr 1, a mammalian myosin I. J. Cell Biol 120, 1393–1403
OpenUrl Abstract/FREE Full Text

[107] Ruppert C.,

[108] Kroschewski R. and

[109] Bahler M.

[110] Saez C. G.,
Myers J. C.,
Shows T. B. and
Leinwand L. A.
(1990). Human nonmuscle myosin heavy chain mRNA: Generation of diversity through alternative polyadenylation. Proc. Nat. Acad. Sci. USA 87, 1164–1168
OpenUrl Abstract/FREE Full Text

[111] Saez C. G.,

[112] Myers J. C.,

[113] Shows T. B. and

[114] Leinwand L. A.

[115] Simons M.,
Wang M.,
McBride O. W.,
Kawamoto S.,
Yamakawa K.,
Gdula D.,
Adelstein R. S. and
Weir L.
(1991). Human nonmuscle myosin heavy chains are encoded by two genes located on different chromosomes. Circul. Res 69, 530–539
OpenUrl Abstract/FREE Full Text

[116] Simons M.,

[117] Wang M.,

[118] McBride O. W.,

[119] Kawamoto S.,

[120] Yamakawa K.,

[121] Gdula D.,

[122] Adelstein R. S. and

[123] Weir L.

[124] Small J. V.
(1994). Microfilament-based motility in non-muscle cells. Curr. Opin. Cell Biol 1, 75–79
OpenUrl

[125] Small J. V.

[126] Strobel M. C.,
Seperack P. K.,
Copeland N. G. and
Jenkins N. A.
(1990). Molecular analysis of two mouse dilute locus deletion mutations: spontaneous dilute lethal205and radiation-induced dilute prenatal lethal Aa2 alleles. Mol. Cell Biol 10, 501–509
OpenUrl Abstract/FREE Full Text

[127] Strobel M. C.,

[128] Seperack P. K.,

[129] Copeland N. G. and

[130] Jenkins N. A.

[131] Sun W. and
Chantler P. D.
(1991). A unique cellular myosin II exhibiting differential expression in the cerebral cortex. Biochem. Biophys. Res. Commun 175, 244–249
OpenUrl CrossRef PubMed

[132] Sun W. and

[133] Chantler P. D.

[134] Warrick H. M. and
Spudich J. A.
(1987). Myosin structure and function in cell motility. Annu. Rev. Cell Biol 3, 379–421
OpenUrl CrossRef Web of Science

[135] Warrick H. M. and

[136] Spudich J. A.

[137] Waterston R. H.
(1989). The minor myosin heavy chain, mhcA, of Caenorhabditis elegans is necessary for the initiation of thick filament assembly. EMBO J 8, 3429–3436
OpenUrl PubMed Web of Science

[138] Waterston R. H.

[139] Zot H. G.,
Doberstein S. K. and
Pollard T. D.
(1992). Myosin-I moves actin filaments on a phospholipid substrate: implications for membrane targeting. J. Cell Biol 116, 367–376
OpenUrl Abstract/FREE Full Text

[140] Zot H. G.,

[141] Doberstein S. K. and

[142] Pollard T. D.

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Summary

REFERENCES

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Cited by...

More in this TOC section

Similar articles

Other journals from The Company of Biologists

Follow us on Instagram

An interview with Derek Walsh

How to improve your scientific writing

Meet the preLighters: Jennifer Ann Black

Mole – The Corona Files

JCS and COVID-19