Faculty Opinions recommendation of Characterization of three full-length human nonmuscle myosin II paralogs.

2014 ◽  
Author(s):  
Miguel Vicente-Manzanares
Keyword(s):  
Myosin Ii ◽  
Full Length ◽  
Nonmuscle Myosin ◽  
Nonmuscle Myosin Ii

scholarly journals Characterization of Three Full-length Human Nonmuscle Myosin II Paralogs

2013 ◽  
Vol 288 (46) ◽  
pp. 33398-33410 ◽  
Author(s):  
Neil Billington ◽  
Aibing Wang ◽  
Jian Mao ◽  
Robert S. Adelstein ◽  
James R. Sellers
Keyword(s):  
Myosin Ii ◽  
Full Length ◽  
Nonmuscle Myosin ◽  
Nonmuscle Myosin Ii

scholarly journals Identification and Characterization of Nonmuscle Myosin II-C, a New Member of the Myosin II Family

2003 ◽  
Vol 279 (4) ◽  
pp. 2800-2808 ◽  
Author(s):  
Eliahu Golomb ◽  
Xuefei Ma ◽  
Siddhartha S. Jana ◽  
Yvette A. Preston ◽  
Sachiyo Kawamoto ◽  
...  
Keyword(s):  
Myosin Ii ◽  
Nonmuscle Myosin ◽  
Nonmuscle Myosin Ii ◽  
Identification And Characterization

scholarly journals Conditional Expression of a Truncated Fragment of Nonmuscle Myosin II-A Alters Cell Shape but Not Cytokinesis in HeLa Cells

2000 ◽  
Vol 11 (10) ◽  
pp. 3617-3627 ◽  
Author(s):  
Qize Wei ◽  
Robert S. Adelstein
Keyword(s):  
Hela Cells ◽  
Fusion Proteins ◽  
Myosin Ii ◽  
Focal Adhesions ◽  
Full Length ◽  
Stress Fibers ◽  
Amino Terminus ◽  
Nonmuscle Myosin ◽  
Nonmuscle Myosin Ii ◽  
Conditional Expression

A truncated fragment of the nonmuscle myosin II-A heavy chain (NMHC II-A) lacking amino acids 1–591, ΔN592, was used to examine the cellular functions of this protein. Green fluorescent protein (GFP) was fused to the amino terminus of full-length human NMHC II-A, NMHC II-B, and ΔN592 and the fusion proteins were stably expressed in HeLa cells by using a conditional expression system requiring absence of doxycycline. The HeLa cell line studied normally expressed only NMHC II-A and not NMHC II-B protein. Confocal microscopy indicated that the GFP fusion proteins of full-length NMHC II-A, II-B, and ΔN592 were localized to stress fibers. However, in vitro assays showed that baculovirus-expressed ΔN592 did not bind to actin, suggesting that ΔN592 was localized to actin stress fibers through incorporation into endogenous myosin filaments. There was no evidence for the formation of heterodimers between the full-length endogenous nonmuscle myosin and truncated nonmuscle MHCs. Expression of ΔN592, but not full-length NMHC II-A or NMHC II-B, induced cell rounding with rearrangement of actin filaments and disappearance of focal adhesions. These cells returned to their normal morphology when expression of ΔN592 was repressed by addition of doxycycline. We also show that GFP-tagged full-length NMHC II-A or II-B, but not ΔN592, were localized to the cytokinetic ring during mitosis, indicating that, in vertebrates, the amino-terminus part of mammalian nonmuscle myosin II may be necessary for localization to the cytokinetic ring.

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