What do contractile proteins do

Research 02 December Structure of the shutdown state of myosin-2 The structure of myosin-2 in the shutdown state reveals how the shutdown state is stabilized and how phosphorylation of light chains allows myosin to be activated.

Nature , Research 19 June Open Access Deconstructing sarcomeric structure—function relations in titin-BioID knock-in mice Titin determines the elasticity of the sarcomere and integrates into both the Z-disc and the M-band.

Nature Communications 11 , Research 24 January Open Access Smoothelin-like 1 deletion enhances myogenic reactivity of mesenteric arteries with alterations in PKC and myosin phosphatase signaling Sara R.

MacDonald Scientific Reports 9 , Research 12 January Open Access Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity Titin regulates myocyte stiffness through uncoiling and unfolding but these two processes cannot fully explain its elasticity.

Nature Communications 9 , Erickson Scientific Reports 7 , Nature Chemistry 2 , Research Highlights 26 March Sticky situation The sliding movement of the actin—myosin protein conjugate responsible for contracting muscles can be inhibited using a dendrimer that glues them together.

Nature Chemistry , 1. Search Search articles by subject, keyword or author. Rapid purification and F-actin cross-linking properties. Biochem J —, J Cell Biol 95; —, Vandekerckhove J, Weber K: At least six different actins are expressed in a higher mammal: An analysis based on the amino acid sequence of the aminoterminal tryptic peptide.

Vandekerckhove J, Weber K: The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle and rabbit slow skeletal muscle. Differentiation —, Dependence on tissue type.

Huxley HE: Structural changes in the actin and myosin containing filaments during contraction. Cummins P, Perry SV: Chemical and immunochemical characteristics of tropomyosins from striated and smooth muscles. Biochem J 43—49, Comp Biochem Physiol 65B: 75—83, FEBS Lett 11—14, J Gen Physiol —, Sobieszek A, Small JV: Regulation of the actin-myosin interaction in vertebrate smooth muscle: Activation via a myosin light-chain kinase and the effect of tropomyosin.

Biochemistry —, J Mol Biol 33—55, Craig R, Smith R, Kendrick-Jones J: Light chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules. Nature Lond —, Ikebe M, Hartshorne DJ: Proteolysis of smooth muscle myosin by Staphylococcus aureus protease: Preparation of heavy meromyosin and subfragment 1 with intact 20,dalton light chains. Sobieszek A: Vertebrate smooth muscle myosin. Enzymatic and structural properties. Baltimore: University Park Press, , pp — Methods Enzymol —, J Biol chem —, J Biochem Tokyo —, Sellers JR, Chock PB, Adelstein RS: The apparently negatively cooperative phosphorylation of smooth muscle myosin at low ionic strength is related to its filamentous state.

Ikebe M, Hartshorne DJ: Phosphorylation of smooth muscle myosin at two distinct sites by myosin light chain kinase. Ikebe M, Hartshorne DJ, Elzinga M: Identification, phosphorylation, and dephosphorylation of a second site for myosin light chain kinase on the 20,dalton light chain of smooth muscle myosin. J Biol Chem 36—39, Haeberle JR, Trockman BA: Two-site phosphoryation of the 20, dalton myosin light chain of glycerinated porcine carotid artery smooth muscle. Biophys J a, Biochem Biophys Res Commun —, FEBS Lett —, Demonstration of an activator.

Kakiuchi S, Yamazaki R, Nakajima H: Properties of a heat-stable phosphodiesterase activating factor isolated from brain extracts. Proc Jpn Acad —, Kretsinger RH: Sttucture and evolution of calcium-modulated proteins. Cheung WY: Calmodulin plays a pivotal role in cellular regulation. Science 19—27, Nature Lond 37—40, A species comparison of cDNA sequences and isolation of a genomic clone. Eur J Biochem —, Kemp BE, Pearson RB: Spatial requirements for location of basic residues in peptide substrates for smooth muscle myosin light chain kinase.

J Biol Chem 25—27, Hardman JG: Cyclic nucleotides and regulation of vascular smooth muscle. J Cardiovasc Pharmacol 6: S—S, Biochim Biophys Acta —, Pato MD, Adelstein RS: Purification and characterizationof a multisubunit phosphatase from turkey gizzard smooth muscle. Walsh MP: Limited proteolysis of smooth muscle myosin light chain kinase.

Biochemistry —, Pato MD, Adelstein RS: Dephosphorylation of the 20,dalton light chain of myosin by two different phosphatases from smooth muscle. Pato MD, Kerc E: Purification and characterization of a smooth muscle myosin phosphatase from turkey gizzards. Other contractile proteins interact with these filaments to create structural rigidity and movement. The structure and function of contractile proteins is striated muscles is well characterized and thus provides a good example for extrapolitation to an analysis of contractile-protein structure and function of nonmuscle cells.

However, the interaction of contractile proteins of various cells may be unique.