NGF-dependent formation of ruffles in PC12D cells required a different pathway from that for neurite outgrowth

Jin, Erika; Nosaka, Kazuto; Sano, Mamoru

doi:10.1016/j.neuint.2007.04.032

Cited by 15 publications

(15 citation statements)

References 50 publications

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“…PKA was able to phosphorylate STEF at three residues (Thr-749, Ser-782, Ser-1562) in vitro, among which Thr-749 was critical for dbcAMP-induced Rac1 activation and neurite extension. Our finding agrees with a previous report that dbcAMP-induced neurite outgrowth in PC12D cells was independent of PI3-kinase (Jin et al , 2007) and argues against the idea that PI3-kinase signaling generally controls axon morphogenesis through the regulation of the cytoskeleton by Rho GTPases (Cosker and Eickholt, 2007; von Philipsborn and Bastmeyer, 2007). …”

Section: Discussionsupporting

confidence: 92%

Phosphorylation of STEF/Tiam2 by protein kinase A is critical for Rac1 activation and neurite outgrowth in dibutyryl cAMP–treated PC12D cells

Goto

Hoshino

Nakamura

2011

MBoC

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Although cAMP-induced neuritogenesis was described in 1975, the signaling pathways from cAMP to cytoskeletal regulation remain elusive. Here we report that the protein kinase A (PKA)-Sif-and Tiam1-like exchange factor (STEF)-Rac1 pathway plays a central role in cytoskeletal regulation during neurite outgrowth in PC12D cells. This result could be extrapolated to axon guidance depending on cAMP signals.

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Section: Discussionsupporting

confidence: 92%

Phosphorylation of STEF/Tiam2 by protein kinase A is critical for Rac1 activation and neurite outgrowth in dibutyryl cAMP–treated PC12D cells

Goto

Hoshino

Nakamura

2011

MBoC

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“…For this, we chose PC12D cells, which express both Cdk5/p35 and AATYK1 [1], [21]. PC12D cells, a subclone of PC12 cells, extend neurites more promptly in response to nerve growth factor (NGF) [22], [23]. We use the term AATYK1 henceforth for endogenous AATYK1 in PC12D cells and brains, as AATYK1A is not distinguishable from AATYK1B using immunoblotting or immunofluorescent staining.…”

Section: Resultsmentioning

confidence: 99%

“…Transfection into COS-7 cells or HEK293 cells was performed using the PolyFect transfection reagent or Lipofectamine 2000, according to the manufacturer's instructions. PC12D cells, which were provided by Dr. Mamoru Sano from the Kyoto Prefectural University of Medicine, were maintained in D-MEM containing 10% fetal bovine serum, 5% horse serum, 100 U/ml penicillin, and 0.1 mg/ml streptomycin [22], [23]. Transfection into PC12D cells was performed using Lipofectamine 2000.…”

Section: Methodsmentioning

confidence: 99%

Phosphorylation of AATYK1 by Cdk5 Suppresses Its Tyrosine Phosphorylation

et al. 2010

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Apoptosis-associated tyrosine kinase 1 (AATYK1), a novel serine/threonine kinase that is highly expressed in the brain, is involved in neurite extension and apoptosis of cerebellar granule neurons; however, its precise function remains unknown. In this study, we investigated the interaction of AATYK1A with Cyclin-dependent kinase 5 (Cdk5)/p35, a proline-directed protein kinase that is predominantly expressed in neurons. AATYK1A bound to the p35 activation subunit of Cdk5 in cultured cells and in mouse brains and colocalized with p35 on endosomes in COS-7 cells. AATYK1A was phosphorylated at Ser34 by Cdk5/p35 in vitro, in cultured neurons and in mouse brain. In PC12D cells, Ser34 phosphorylation increased after treatment with nerve growth factor and phosphorylated AATYK1A accumulated in growth cones of PC12D cells. Ser34 phosphorylation suppressed the tyrosine phosphorylation of AATYK1A by Src family kinases. These results suggest a possibility that AATYK1A plays a role in early to recycling endosomes and its function is regulated by phosphorylation with Cdk5 or Src-family kinases.

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“…NGF-induced cell extension in PC12 cells requires APC (Dobashi et al, 2000) and involves inhibition of GSK-3b (Jin et al, 2007), similarly to axonal outgrowth in ex vivo neuronal cultures and directional cell migration in other cell types (Etienne-Manneville and Hall, 2003;Zhou et al, 2004). We have shown previously that APC clusters localize to the tip of neurite extensions after prolonged (1-2 day) NGF signaling (Votin et al, 2005).…”

Section: Ngf-and Egf-induced Cell Extension Promotes Apc Clustering Amentioning

confidence: 83%

Mitogen-activated protein kinase (MAPK/ERK) regulates adenomatous polyposis coli during growth-factor-induced cell extension

Caro-Gonzalez

Nejsum

Siemers

et al. 2012

Journal of Cell Science

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SummaryRegulation of the microtubule-and actin-binding protein adenomatous polyposis coli (APC) is crucial for the formation of cell extensions in many cell types. This process requires inhibition of glycogen synthase kinase-3b (GSK-3b), which otherwise phosphorylates APC and decreases APC-mediated microtubule bundling. Although it is assumed, therefore, that APC phosphorylation is decreased during initiation of cell extensions, the phosphorylation state of APC has never been analyzed directly. We show here that NGF-and EGF-induced initial cell extensions result in APC phosphorylation by the MAPK/ERK pathway, which, in parallel with inhibition of GSK-3b, promotes localization of APC to the tip of cell extensions. Whereas GSK-3b inhibition promotes APC binding and stabilization of microtubules, we show that phosphorylation by ERK inhibits the interaction of APC with F-actin, and APCmediated F-actin bundling, but not APC-mediated microtubule bundling, in vitro. These results identify a previously unknown APC regulatory pathway during growth-factor-induced cell extension, and indicate that the GSK-3b and ERK pathways act in parallel to regulate interactions between APC and the cytoskeleton during the formation of cell extensions.

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NGF-dependent formation of ruffles in PC12D cells required a different pathway from that for neurite outgrowth

Cited by 15 publications

References 50 publications

Phosphorylation of STEF/Tiam2 by protein kinase A is critical for Rac1 activation and neurite outgrowth in dibutyryl cAMP–treated PC12D cells

Phosphorylation of STEF/Tiam2 by protein kinase A is critical for Rac1 activation and neurite outgrowth in dibutyryl cAMP–treated PC12D cells

Phosphorylation of AATYK1 by Cdk5 Suppresses Its Tyrosine Phosphorylation

Mitogen-activated protein kinase (MAPK/ERK) regulates adenomatous polyposis coli during growth-factor-induced cell extension

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