Caldesmon and the Regulation of Cytoskeletal Functions

Wang, C. L. Albert

doi:10.1007/978-0-387-85766-4_19

Cited by 45 publications

(44 citation statements)

References 198 publications

(199 reference statements)

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“…In conclusion, RSP2 is comprised of multiple modules, like calmodulin-binding proteins in the actin cytoskeletal system (59). In the case of RSP2, the D/D domain docks a helix for RS assembly, and its special calmodulin-binding tail modulates the spokehead, enabling the biflagellate green alga to steer in a unique situation.…”

Section: Discussionmentioning

confidence: 98%

The DPY-30 Domain and Its Flanking Sequence Mediate the Assembly and Modulation of Flagellar Radial Spoke Complexes

Gopal

Foster

Yang

2012

Molecular and Cellular Biology

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In both deletion transgenic strains, the subunits near the spokehead were restored, but their firm attachment to the spokestalk required the DPY-30 domain. We postulate that the DPY-30 -helix dimer is a conserved two-prong linker, required for normal motility, organizing duplicated subunits in the radial spoke stalk and formation of a symmetrical spokehead. Further, the dispensable calmodulin-binding region appears to fine-tune the spokehead for regulation of "steering" motility in the green algae. Thus, in general, D/D domains may function to localize molecular modules for both the assembly and modulation of macromolecular complexes.

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Section: Discussionmentioning

confidence: 98%

The DPY-30 Domain and Its Flanking Sequence Mediate the Assembly and Modulation of Flagellar Radial Spoke Complexes

Gopal

Foster

Yang

2012

Molecular and Cellular Biology

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“…Twenty to forty micrograms of the tissue lysates were subjected to SDS-PAGE and transferred to a nitrocellulose membrane at 100 V for 1 h and 15 min at 4°C, as previously described in detail (56,57). Briefly, the membranes were blocked and then incubated in primary antibodies against active, phosphorylated MAP kinase (1:5,000, Promega, Madison, WI) and total p42/p44 MAP kinase (1:1,000, Millipore, Billerica, MA); Thr 38 -phosphorylated CPI-17 (1:100, Santa Cruz Biotechnology, Santa Cruz, CA) and total CPI-17 (1:400, Santa Cruz Biotechnology); Ser 359 -MKP-1 phosphorylation (1:1,000, Abcam, Cambridge, MA) and total MKP-1 (1:1,000, Abcam); or Ser 789 -caldesmon phosphorylation (1:1,000, Millipore) and total caldesmon (1:5,000, Sigma-Aldrich) overnight at 4°C.…”

Section: Methodsmentioning

confidence: 99%

“…Caldesmon is a known substrate for MAP kinase (1,20,42,56). We determined caldesmon phosphorylation levels at Ser 789 , the site catalyzed by MAP kinase.…”

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confidence: 99%

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Regulation of mitogen-activated protein kinase by protein kinase C and mitogen-activated protein kinase phosphatase-1 in vascular smooth muscle

Trappanese

Sivilich

Ets

et al. 2016

American Journal of Physiology-Cell Physiology

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Trappanese DM, Sivilich S, Ets HK, Kako F, Autieri MV, Moreland RS. Regulation of mitogen-activated protein kinase by protein kinase C and mitogen-activated protein kinase phosphatase-1 in vascular smooth muscle. Am J Physiol Cell Physiol 310: C921-C930, 2016. First published April 6, 2016; doi:10.1152/ajpcell.00311.2015.-Vascular smooth muscle contraction is primarily regulated by phosphorylation of myosin light chain. There are also modulatory pathways that control the final level of force development. We tested the hypothesis that protein kinase C (PKC) and mitogen-activated protein (MAP) kinase modulate vascular smooth muscle activity via effects on MAP kinase phosphatase-1 (MKP-1). Swine carotid arteries were mounted for isometric force recording and subjected to histamine stimulation in the presence and absence of inhibitors of PKC [bisindolylmaleimide-1 (Bis)], MAP kinase kinase (MEK) (U0126), and MKP-1 (sanguinarine) and flash frozen for measurement of MAP kinase, PKC-potentiated myosin phosphatase inhibitor 17 (CPI-17), and caldesmon phosphorylation levels. CPI-17 was phosphorylated in response to histamine and was inhibited in the presence of Bis. Caldesmon phosphorylation levels increased in response to histamine stimulation and were decreased in response to MEK inhibition but were not affected by the addition of Bis. Inhibition of PKC significantly increased p42 MAP kinase, but not p44 MAP kinase. Inhibition of MEK with U0126 inhibited both p42 and p44 MAP kinase activity. Inhibition of MKP-1 with sanguinarine blocked the Bis-dependent increase of MAP kinase activity. Sanguinarine alone increased MAP kinase activity due to its effects on MKP-1. Sanguinarine increased MKP-1 phosphorylation, which was inhibited by inhibition of MAP kinase. This suggests that MAP kinase has a negative feedback role in inhibiting MKP-1 activity. Therefore, PKC catalyzes MKP-1 phosphorylation, which is reversed by MAP kinase. Thus the fine tuning of vascular contraction is due to the concerted effort of PKC, MAP kinase, and MKP-1.bisindolylmaleimide-1; U0126; sanguinarine; caldesmon; CPI-17; phos-tag gel electrophoresis EXTRACELLULAR SIGNAL-REGULATED kinase 1/2 mitogen-activated protein kinase (MAP kinase; also known as p42/p44 MAP kinase) is a serine/threonine protein kinase that has been identified in several types of smooth muscle (7,10,19). MAP kinase is activated via dual phosphorylation of Thr 187 and Tyr 185 catalyzed by MAP kinase kinase (MEK) and has been shown to play a significant role in activating several proteins required for cell growth in proliferating dedifferentiated smooth muscle cells (24,26). However, the role of MAP kinase in differentiated, contractile smooth muscle cells is not as well understood.In differentiated smooth muscle, it has been suggested that MAP kinase may be involved in calcium-independent regulation of smooth muscle contraction (17). MAP kinase has been shown to phosphorylate the thin filament protein caldesmon and relieve its inhibitory action on the actin-activated myosin ATPase, ...

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“…Caldesmon is a thin filament-associated actin-, myosin-, tropomyosin-, and calmodulin-binding protein (for review see Sobue and Sellers 1991;Huber 1997;Dabrowska et al 2004;Wang 2008). Low-molecularmass isoforms of caldesmon (l-caldesmon, 70 to 80 kDa) are thought to be widely distributed in nonmuscle tissues, but only a few studies have used immunohistochemistry to investigate the distribution of caldesmon in selected tissues Fujita et al 1984;Ishimura et al 1984).…”

Section: Introductionmentioning

confidence: 99%

The Actin-binding Protein Caldesmon Is in Spleen and Lymph Nodes Predominately Expressed by Smooth-muscle Cells, Reticular Cells, and Follicular Dendritic Cells

Köhler

2009

J Histochem Cytochem.

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Reticular cells and follicular dendritic cells (FDCs) build up a framework that underlies the compartmentalization of spleens and lymph nodes. Subpopulations of reticular cells express the smooth-muscle isoform of actin, indicative of a specialized contractile apparatus. We have investigated the distribution of the actin-binding protein caldesmon in spleen and lymph nodes of mice and rats. Caldesmon modulates contraction and regulates cell motility. Alternative splicing of transcripts from a single gene results in high-molecular-mass isoforms ( h-caldesmon) that are predominately expressed by smooth-muscle cells (SMCs), and low-molecular-mass isoforms ( I-caldesmon) that are thought to be widely distributed in non-muscle tissues, but the distribution of caldesmon in spleen and lymph nodes has not been reported. We have performed Western blot analysis and immunohistochemistry using four different antibodies against caldesmon, among these a newly developed polyclonal antibody directed against recombinant mouse caldesmon. Western blot analysis showed the preponderance of I-caldesmon in spleen and lymph nodes. Our results from immunohistochemistry demonstrate caldesmon in SMCs, as expected, but also in reticular cells and FDCs, and suggest that the isoform highly expressed by reticular cells is I-caldesmon. In spleen of SCID mice, caldesmon was expressed by reticular cells in the absence of lymphocytes.

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Caldesmon and the Regulation of Cytoskeletal Functions

Cited by 45 publications

References 198 publications

The DPY-30 Domain and Its Flanking Sequence Mediate the Assembly and Modulation of Flagellar Radial Spoke Complexes

The DPY-30 Domain and Its Flanking Sequence Mediate the Assembly and Modulation of Flagellar Radial Spoke Complexes

Regulation of mitogen-activated protein kinase by protein kinase C and mitogen-activated protein kinase phosphatase-1 in vascular smooth muscle

The Actin-binding Protein Caldesmon Is in Spleen and Lymph Nodes Predominately Expressed by Smooth-muscle Cells, Reticular Cells, and Follicular Dendritic Cells

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