Association of CPI-17 with protein kinase C and casein kinase I

Zemlickova, Eva; Johannes, Franz‐Josef; Aitken, Alastair; Dubois, Thierry

doi:10.1016/j.bbrc.2004.02.014

Cited by 31 publications

(19 citation statements)

References 36 publications

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“…Here we observed that noncanonical Wnt signaling, mediated by Fmi-Fz8, restricts NFAT nuclear translocation either through controlling intracellular Ca 2+ level, potentially through inhibition of LTCC, or via Cdc42-Pak1-CK1α pathway in HSCs. The two events are also very possibly linked because it was reported that CK1α activity can be suppressed by Ca 2+ -dependent PKC (Zemlickova et al, 2004). Further studies are required to address whether LTCC is functionally required and whether Ca 2+ through PKC regulates CK1α in HSCs.…”

Section: Discussionmentioning

confidence: 97%

Noncanonical Wnt Signaling Maintains Hematopoietic Stem Cells in the Niche

Sugimura

Venkatraman

et al. 2012

Cell

267

238

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SUMMARY Wnt signaling is involved in self-renewal and maintenance of hematopoietic stem cells (HSCs); however, the particular role of noncanonical Wnt signaling in regulating HSCs in vivo is largely unknown. Here, we show Flamingo (Fmi) and Frizzled (Fz) 8, members of noncanonical Wnt signaling, both express in and functionally maintain quiescent long-term HSCs. Fmi regulates Fz8 distribution at the interface between HSCs and N-cadherin+ osteoblasts (N-cad+OBs that enrich osteoprogenitors) in the niche. We further found that N-cad+OBs predominantly express noncanonical Wnt ligands and inhibitors of canonical Wnt signaling under homeostasis. Under stress, noncanonical Wnt signaling is attenuated and canonical Wnt signaling is enhanced in activation of HSCs. Mechanistically, noncanonical Wnt signaling mediated by Fz8 suppresses the Ca2+-NFAT- IFNγ pathway, directly or indirectly through the CDC42-CK1α complex and also antagonizes canonical Wnt signaling in HSCs. Taken together, our findings demonstrate that noncanonical Wnt signaling maintains quiescent long-term HSCs through Fmi and Fz8 interaction in the niche.

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Section: Discussionmentioning

confidence: 97%

Noncanonical Wnt Signaling Maintains Hematopoietic Stem Cells in the Niche

Sugimura

Venkatraman

et al. 2012

Cell

267

238

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“…While PKCα and PKCδ are the primary kinases for CPI-17 phosphorylation in response to agonist stimulation, CPI-17 can also bind to the regulatory domain of PKC isoforms, including α, and the "non-traditional" PKCs ε, λ, ζ, and μ. 55 Zipper-interacting kinase (ZIPK) and p21-activated kinase can also directly phosphorylate isolated CPI-17 at T38. 56,57 Phosphorylated CPI-17 selectively inhibits MLCP with an IC 50 value of approximately 1 nM, due to the association of the PPP1Cδ catalytic subunit with MYPT1.…”

Section: Inhibition Of Myosin Light Chain Phosphatase Activity By Cpimentioning

confidence: 99%

Calcium Sensitization Mechanisms in Gastrointestinal Smooth Muscles

Perrino

2016

J Neurogastroenterol Motil

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An increase in intracellular Ca2+ is the primary trigger of contraction of gastrointestinal (GI) smooth muscles. However, increasing the Ca 2+ sensitivity of the myofilaments by elevating myosin light chain phosphorylation also plays an essential role. Inhibiting myosin light chain phosphatase activity with protein kinase C-potentiated phosphatase inhibitor protein-17 kDa (CPI-17) and myosin phosphatase targeting subunit 1 (MYPT1) phosphorylation is considered to be the primary mechanism underlying myofilament Ca 2+ sensitization. The relative importance of Ca 2+ sensitization mechanisms to the diverse patterns of GI motility is likely related to the varied functional roles of GI smooth muscles. Increases in CPI-17 and MYPT1 phosphorylation in response to agonist stimulation regulate myosin light chain phosphatase activity in phasic, tonic, and sphincteric GI smooth muscles. Recent evidence suggests that MYPT1 phosphorylation may also contribute to force generation by reorganization of the actin cytoskeleton. The mechanisms responsible for maintaining constitutive CPI-17 and MYPT1 phosphorylation in GI smooth muscles are still largely unknown. The characteristics of the cell-types comprising the neuroeffector junction lead to fundamental differences between the effects of exogenous agonists and endogenous neurotransmitters on Ca 2+ sensitization mechanisms. The contribution of various cell-types within the tunica muscularis to the motor responses of GI organs to neurotransmission must be considered when determining the mechanisms by which Ca 2+ sensitization pathways are activated. The signaling pathways regulating Ca 2+ sensitization may provide novel therapeutic strategies for controlling GI motility. This article will provide an overview of the current understanding of the biochemical basis for the regulation of Ca

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“…We also quantified protein kinase C and CPI-17 (protein kinase C potentiated inhibitor protein 17) expression in human lung tissue, by using anti-mouse PKCα (BD Biosciences) and/or anti-mouse PKCδ antibody (BD Biosciences), anti-rabbit CPI-17 antibody (Epitomics). 18,19 Signaling was visualized with an ECL detection kit.…”

Section: Protocolmentioning

confidence: 99%

“…Immunostaining was performed using antimouse ROCK1 antibody (BD Biosciences), anti-mouse ROCK2 antibody (BD Biosciences), anti-rabbit phospho-MBS antibody (Upstate, Tokyo, Japan) and anti-mouse MBS antibody (BD Biosciences), [20][21][22] and CPI-17 antibody (Epitomics). 18,19 Diaminobebzidine and hydrogen dioxide were applied to develop color. Immunostraining was performed by the biotin-avidin complex method (Histofine SAB-PO(M) Kit/SAB-PO(R) Kit).…”

Section: Protocolmentioning

confidence: 99%