Role of the C‐terminal extremities of the smooth muscle myosin heavychains" implication for assembly properties

Quevillon‐Chéruel, Sophie; Foucault, G.; Desmadril, Michel; Lompré, Anne‐Marie; Béchet, Jean‐Jacques

doi:10.1016/s0014-5793(99)00827-3

Cited by 5 publications

(1 citation statement)

References 28 publications

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“…Assembly of myosin IIB was significantly inhibited by the phosphoryltaion of its nonhelical tail piece ( , ). The alternatively spliced isoforms of smooth muscle myosin heavy chains that differ at their nonhelical tail pieces exhibited different properties during filament assembly ( , ). The filament assembly of Dictyostelium myosin II is regulated by phosphorylation at three Thr residues in the tail region ( − ).…”

Section: Discussionmentioning

confidence: 99%

Critical Regions for Assembly of Vertebrate Nonmuscle Myosin II

et al. 2004

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Myosin II molecules assemble and form filaments through their C-terminal rod region, and the dynamic filament assembly-disassembly process of nonmuscle myosin II molecules is important for cellular activities. To estimate the critical region for filament formation of vertebrate nonmuscle myosin II, we assessed the solubility of a series of truncated recombinant rod fragments of nonmuscle myosin IIB at various concentrations of NaCl. A C-terminal 248-residue rod fragment (Asp 1729-Glu 1976) was shown by its solubility behavior to retain native assembly features, and two regions within it were found to be necessary for assembly: 35 amino acid residues from Asp 1729 to Thr 1763 and 39 amino acid residues from Ala 1875 to Ala 1913, the latter containing a sequence similar to the assembly competence domain (ACD) of skeletal muscle myosin. Fragments lacking either of the two regions were soluble at any NaCl concentration. We referred to these two regions as nonmuscle myosin ACD1 (nACD1) and nACD2, respectively. In addition, we constructed an alpha-helical coiled-coil model of the rod fragment, and found that a remarkable negative charge cluster (termed N1) and a positive charge cluster (termed P2) were present within nACD1 and nACD2, respectively, besides another positive charge cluster (termed P1) in the amino-terminal vicinity of nACD2. From these results, we propose two major electrostatic interactions that are essential for filament formation of nonmuscle myosin II: the antiparallel interaction between P2 and N1 which is essential for the nucleation step and the parallel interaction between P1 and N1 which is important for the elongation step.

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Section: Discussionmentioning

confidence: 99%

Critical Regions for Assembly of Vertebrate Nonmuscle Myosin II

et al. 2004

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Smooth-Muscle Myosin II

Cremo

Hartshorne

Proteins and Cell Regulation

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Mutations in myosin heavy chain 11 cause a syndrome associating thoracic aortic aneurysm/aortic dissection and patent ductus arteriosus

Zhu¹,

Vranckx²,

Kien³

et al. 2006

Nat Genet

552

401

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We have recently described two kindreds presenting thoracic aortic aneurysm and/or aortic dissection (TAAD) and patent ductus arteriosus (PDA) and mapped the disease locus to 16p12.2-p13.13 (ref. 3). We now demonstrate that the disease is caused by mutations in the MYH11 gene affecting the C-terminal coiled-coil region of the smooth muscle myosin heavy chain, a specific contractile protein of smooth muscle cells (SMC). All individuals bearing the heterozygous mutations, even if asymptomatic, showed marked aortic stiffness. Examination of pathological aortas showed large areas of medial degeneration with very low SMC content. Abnormal immunological recognition of SM-MHC and the colocalization of wild-type and mutant rod proteins in SMC, in conjunction with differences in their coimmunoprecipitation capacities, strongly suggest a dominant-negative effect. Human MYH11 gene mutations provide the first example of a direct change in a specific SMC protein leading to an inherited arterial disease.

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Role of the C‐terminal extremities of the smooth muscle myosin heavychains" implication for assembly properties

Cited by 5 publications

References 28 publications

Critical Regions for Assembly of Vertebrate Nonmuscle Myosin II

Critical Regions for Assembly of Vertebrate Nonmuscle Myosin II

Smooth-Muscle Myosin II

Mutations in myosin heavy chain 11 cause a syndrome associating thoracic aortic aneurysm/aortic dissection and patent ductus arteriosus

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