Protein Kinase D regulates several aspects of development in Drosophila melanogaster

Maier, Dieter; Nagel, Anja C.; Helena, Gloc; Haußer, Angelika; Kugler, Sabrina J.; Wech, Irmgard; Preiss, Anette

doi:10.1186/1471-213x-7-74

Cited by 19 publications

(31 citation statements)

References 51 publications

(88 reference statements)

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“…Hence, Drosophila Ssh does not contain the sequence recognition site that was identified in SSH1L as target of human PKD. However, we have noted before that manipulation of Drosophila PKD activity affected the development of different organs in a way that conforms to a role of PKD in the regulation of actin dynamics in Drosophila as well (Maier et al 2006, 2007).…”

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confidence: 70%

“…The following fly stocks were used: UAS‐PKD‐SE 139‐2 ‐GFP (Maier et al 2007); FRT82B ssh 1‐63 / TM3 Ser; UAS‐ssh.N 30 , UAS‐ssh.CS 11 (Niwa et al 2002); y w , FRT82B ubi‐GFP /TM6B; y w hs‐flp; act>CD2>Gal4, UAS‐GFPnls / TM6B (Struhl and Basler 1993; kindly obtained from K. Basler); UAS‐lacZ, gmr‐Gal4; y 1 w 67c23 . Flies were obtained from the Bloomington fly collection if not noted otherwise.…”

Section: Methodsmentioning

confidence: 99%

“…The dark patches may result from secretion defects as a consequence of PKD-SE overexpression ( Fig. 1f; MAIER et al 2007).…”

Section: Drosophila Pkd-se Induces Phenotypes Comparable To the Loss mentioning

confidence: 99%

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Constitutively active Protein kinase D acts as negative regulator of the Slingshot-phosphatase in Drosophila

et al. 2010

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The mammalian protein kinase D family is involved in manifold cellular processes including cell migration and motility. Recently it was shown that human PKD1 and PKD2 phosphorylate and thereby inhibit Slingshot 1 Like (SSH1L), a phosphatase which is central to the regulation of actin cytoskeletal dynamics. We noted before that the overexpression of a constitutively active form of Drosophila PKD (PKD-SE) affects the fly retina and the resultant phenotypes suggest underlying defects in the actin cytoskeleton. Drosophila Slingshot, however, does not possess the phosphorylation site known to be targeted in SSH1L by human PKD1. Here we show that Drosophila PKD, despite this lack of conservation, nevertheless negatively regulates Slingshot. Overexpression of the active PKD-SE protein causes cellular defects that are similar to those of slingshot mutants. These include aberrant bristle morphology and positioning of photoreceptor nuclei. Interestingly, the observed nuclear mispositioning is due to a disturbance of the cytoskeleton rather than the epithelial organization. In accordance, overexpression of PKD-SE results in an accumulation of filamentous actin. This enrichment is modified by changes in slingshot gene doses, in line with an antagonistic relationship between PKD and slingshot. We conclude that similar to mammals, Drosophila PKD is a negative regulator of Ssh, with the premise of a different target phosphorylation site in Ssh.

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confidence: 70%

Section: Methodsmentioning

confidence: 99%

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Constitutively active Protein kinase D acts as negative regulator of the Slingshot-phosphatase in Drosophila

et al. 2010

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“…Here, the C‐terminus of SSH lacks the two PKD phospho‐sites, whereas the previously identified phosphorylation site at Ser 477 (Ser 402 in mammals) is conserved (Fig 4A; Ohta et al , 2003). Similarly to the human PKD1ca protein, Drosophila PKDca‐GFP (Maier et al , 2007) displayed constitutive activity (supplementary Fig S1 online). In in vitro kinase assays, Drosophila PKDca was able to directly phosphorylate a truncated Drosophila SSH–GST‐fusion protein comprising the amino acids 461–671 (Fig 4B).…”

Section: Resultsmentioning

confidence: 99%

Phosphorylation of Ser 402 impedes phosphatase activity of slingshot 1

et al. 2011

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By using mass spectrometry, we have identified Ser 402 as a new phosphorylation site within the catalytic domain of human slingshot 1 (SSH1). Phosphorylation at this site inhibits substrate binding and, thus, phosphatase activity in vitro, resulting in enrichment of phosphorylated cofilin in monolayer cell culture. We further demonstrate that protein kinase D (PKD) is upstream from Ser 402 phosphorylation. Accordingly, expression of active PKD in Drosophila phenotypically mimics the loss of SSH activity by inducing accumulation of phosphorylated cofilin and filamentous actin. We thus identify a universal mechanism by which PKD controls SSH1 phosphatase activity.

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“…Thus, other factors likely regulate HSV‐1 egress at the TGN in addition to PKD. Similarly, the impact of the PKD1 kinase dead mutant on HSV‐1 egress in 143B cells, which only express PKD3, hints at a partial complementarity among the different PKD isoforms (34,35). Furthermore, the implication of PKD in HSV‐1 egress is significant since detected in two independent cell types.…”

Section: Discussionmentioning

confidence: 99%

Protein Kinase D‐Dependent Trafficking of the Large Herpes simplex Virus Type 1 Capsids from the TGN to Plasma Membrane

Rémillard-Labrosse

Mihai

Duron

et al. 2009

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Protein Kinase D regulates several aspects of development in Drosophila melanogaster

Cited by 19 publications

References 51 publications

Constitutively active Protein kinase D acts as negative regulator of the Slingshot-phosphatase in Drosophila

Constitutively active Protein kinase D acts as negative regulator of the Slingshot-phosphatase in Drosophila

Phosphorylation of Ser 402 impedes phosphatase activity of slingshot 1

Protein Kinase D‐Dependent Trafficking of the Large Herpes simplex Virus Type 1 Capsids from the TGN to Plasma Membrane

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