MLCK-A, an unconventional myosin light chain kinase from
            <i>Dictyostelium</i>
            , is activated by a cGMP-dependent pathway

Silveira, Linda A.; Smith, Janet L.; Tan, John L.; Spudich, James A.

doi:10.1073/pnas.95.22.13000

Cited by 21 publications

(16 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, activation of PKG could lead to either attraction or repulsion, depending possibly on the interplay of intracellular signaling pathways (Nishiyama et al, 2003). PKG may affect ion channels, Ca 2+ release, and myosin contractility to regulate growth cone motility (Silveira et al, 1998; Hofmann et al, 2000). Our findings are consistent with the idea that PKG signaling is important in growth cone guidance (Ming et al, 1997; Song et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

A subset of signal transduction pathways is required for hippocampal growth cone collapse induced by ephrin‐A5

Yue

Dreyfus

Kong

et al. 2008

Developmental Neurobiology

View full text Add to dashboard Cite

The Eph family tyrosine kinase receptors and their ligands, ephrins, play key roles in a wide variety of physiological and pathological processes including tissue patterning, angiogenesis, bone development, carcinogenesis, axon guidance, and neural plasticity. However, the signaling mechanisms underlying these diverse functions of Eph receptors have not been well understood. In this study, effects of Eph receptor activation on several important signal transduction pathways are examined. In addition, the roles of these pathways in ephrin-A5-induced growth cone collapse were assessed with a combination of biochemical analyses, pharmacological inhibition, and overexpression of dominant-negative and constitutively active mutants. These analyses showed that ephrin-A5 inhibits Erk activity while activates c-Jun N-terminal kinase. However, regulation of these two pathways is not required for ephrin-A5-induced growth cone collapse in hippocampal neurons. Artificial Erk activation by expression of constitutively active Mek1 and B-Raf failed to block ephrin-A5 effects on growth cones, and inhibitors of the Erk pathway also failed to inhibit collapse by ephrin-A5. Inhibition of JNK had no effects on ephrin-A5-induced growth cone collapse either. In addition, inhibitors to PKA and PI3-K showed no effects on ephrin-A5-induced growth cone collapse. However, pharmacological blockade of phosphotyrosine phosphatase activity, the Src family kinases, cGMP-dependent protein kinase, and myosin light chain kinase significantly inhibited ephrin-A5-induced growth cone collapse. These observations indicate that only a subset of signal transduction pathways is required for ephrin-A5-induced growth cone collapse.

show abstract

Section: Discussionmentioning

confidence: 99%

A subset of signal transduction pathways is required for hippocampal growth cone collapse induced by ephrin‐A5

Yue

Dreyfus

Kong

et al. 2008

Developmental Neurobiology

View full text Add to dashboard Cite

show abstract

“…cGMP plays an important role in Dictyostelium chemotaxis, and is predominantly produced by a soluble guanylate cyclase [146,147,152,153]. Evidence for a regulatory role of cGMP in the function of myosin II includes the identification of an MLCK that is indirectly activated by cGMP, involving GbpC (cGMP-binding protein C) [154][155][156][157]. This suggests that, in addition to promoting the abovementioned assembly of actin-myosin filaments, cGMP also regulates the phosphorylation-dependent motor activity of myosin II.…”

Section: Regulation Of Actin-myosin Assemblymentioning

confidence: 99%

Big roles for small GTPases in the control of directed cell movement

Charest

Firtel

2006

Biochemical Journal

179

156

View full text Add to dashboard Cite

Small GTPases are involved in the control of diverse cellular behaviours, including cellular growth, differentiation and motility. In addition, recent studies have revealed new roles for small GTPases in the regulation of eukaryotic chemotaxis. Efficient chemotaxis results from co-ordinated chemoattractant gradient sensing, cell polarization and cellular motility, and accumulating data suggest that small GTPase signalling plays a central role in each of these processes as well as in signal relay. The present review summarizes these recent findings, which shed light on the molecular mechanisms by which small GTPases control directed cell migration.

show abstract

“…This kinase directly or indirectly phosphorylates myosin light-chain-specific protein kinase and myosin heavy-chain-specific protein kinase C, which in turn phosphorylate the different myosins, resulting in rearrangements of myosin filaments necessary for movement [14][15][16][17][18][19].…”

Section: Introductionmentioning

confidence: 99%

Guanylate cyclase in Dictyostelium discoideum with the topology of mammalian adenylate cyclase

Roelofs

Snippe

Kleineidam

et al. 2001

Biochemical Journal

View full text Add to dashboard Cite

The core of adenylate and guanylate cyclases is formed by an intramolecular or intermolecular dimer of two cyclase domains arranged in an antiparallel fashion. Metazoan membrane-bound adenylate cyclases are composed of 12 transmembrane spanning regions, and two cyclase domains which function as a heterodimer and are activated by G-proteins. In contrast, membrane-bound guanylate cyclases have only one transmembrane spanning region and one cyclase domain, and are activated by extracellular ligands to form a homodimer. In the cellular slime mould, Dictyosteliumdiscoideum, membrane-bound guanylate cyclase activity is induced after cAMP stimulation; a G-protein-coupled cAMP receptor and G-proteins are essential for this activation. We have cloned a Dictyostelium gene, DdGCA, encoding a protein with 12 transmembrane spanning regions and two cyclase domains. Sequence alignment demonstrates that the two cyclase domains are transposed, relative to these domains in adenylate cyclases. DdGCA expressed in Dictyostelium exhibits high guanylate cyclase activity and no detectable adenylate cyclase activity. Deletion of the gene indicates that DdGCA is not essential for chemotaxis or osmo-regulation. The knock-out strain still exhibits substantial guanylate cyclase activity, demonstrating that Dictyostelium contains at least one other guanylate cyclase.

show abstract

MLCK-A, an unconventional myosin light chain kinase from Dictyostelium , is activated by a cGMP-dependent pathway

Abstract: ABSTRACT

Cited by 21 publications

References 56 publications

A subset of signal transduction pathways is required for hippocampal growth cone collapse induced by ephrin‐A5

A subset of signal transduction pathways is required for hippocampal growth cone collapse induced by ephrin‐A5

Big roles for small GTPases in the control of directed cell movement

Guanylate cyclase in Dictyostelium discoideum with the topology of mammalian adenylate cyclase

Contact Info

Product

Resources

About