Ca 2+ /calmodulin-dependent protein kinase phosphatase (CaMKP/PPM1F) interacts with neurofilament L and inhibits its filament association

Ozaki, Hana; Katoh, Tsuyoshi; Nakagawa, Ryoko; Ishihara, Yasuhiro; Sueyoshi, Noriyuki; Kameshita, Isamu; Taniguchi, Tadatsugu; Hirano, Tetsuo; Yamazaki, Takeshi; Ishida, Atsuhiko

doi:10.1016/j.bbrc.2016.06.141

Cited by 7 publications

(5 citation statements)

References 22 publications

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“…Protein phosphatase Mg2+/Mn2+‐dependent 1F (PPM1F), a Ser/Thr protein phosphatase that belongs to PPM family has been reported to exhibit cellular functions by repressing filament association and affecting cell polarity and centrosome placement . Moreover, PPM1F (also known as POPX2) promotes cancer cell motility and invasiveness through the regulation of the GSK/β‐catenin and MAPK1/3 pathways, and accelerates smoking‐caused breast cancer by inactivating p53 signals, indicating a prognostic target for cancer prevention and therapy …”

Section: Introductionmentioning

confidence: 99%

Loss of PPM1F expression predicts tumour recurrence and is negatively regulated by miR‐590‐3p in gastric cancer

et al. 2018

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Section: Introductionmentioning

confidence: 99%

Loss of PPM1F expression predicts tumour recurrence and is negatively regulated by miR‐590‐3p in gastric cancer

et al. 2018

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“…PPM1F regulates physiological and pathological processes in organisms by regulating kinases or interacting with other proteins [34]. Previous studies have shown that PPM1F interacts with NFL to inhibit the formation of large lamentous aggregates and regulate the neuro lament network during neuronal differentiation [20]. PPM1F interacts with effectors and regulators of Rho GTPase and is involved in the regulation of the actin cytoskeleton, which in turn affects cell shape and migration [35][36][37].…”

Section: Discussionmentioning

confidence: 99%

“…PPM phosphatases regulate cell cycle, cell differentiation, immune response, and cell metabolism [18]. Mutations, overexpression, or deletion of the PPM phosphatase gene result in aberrant cellular responses that lead to a variety of human diseases [19,20].…”

Section: Introductionmentioning

confidence: 99%

PPM1F regulates ovarian cancer progression by affecting the dephosphorylation of ITGB1

Leng,

Li,

et al. 2023

Preprint

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Background PPM1F has been shown to play diverse biological functions in the progression of multiple tumors. PPM1F controls the T788/T789 phosphorylation switch of ITGB1 and regulates integrin activity. However, the impacts of PPM1F and ITGB1 on ovarian cancer (OV) progression remain unclear. whether there is such a regulatory relationship between PPM1F and ITGB1 in ovarian cancer has not been studied. Therefore, the purpose of this study is to elucidate the function and mechanism of PPM1F in ovarian cancer. Methods The expression level and survival curve of PPM1F were analyzed by databases. Gain of function and loss of function were applied to explore the function of PPM1F in ovarian cancer. Tumor formation assay in nude mice showed that knockdown of PPM1F inhibited tumor formation. We testified the effect of PPM1F on ITGB1 dephosphorylation in ovarian cancer cells by co-immunoprecipitation and western blotting. Loss of function was applied to investigate the function of ITGB1 in ovarian cancer. ITGB1-mut overexpression promotes the progression of ovarian cancer. Rescue assays showed the promoting effect of ITGB1-wt on ovarian cancer is attenuated due to the dephosphorylation of ITGB1-wt by PPM1F. Results PPM1F and ITGB1 play an oncogene function in ovarian cancer. PPM1F regulates the phosphorylation of ITGB1, which affects the occurrence and development of ovarian cancer.

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“…The binding partners of POPX2 Table 1 summarizes known binding partners of POPX2, their cellular roles, and signaling pathways which they are implicated 6,7,12,15,[17][18][19][20][21][22][23] . The major functions regulated by POPX2 and its binding partners are further discussed below.…”

Section: Exploring the Functions Of Popx2 Through Its Interactomementioning

confidence: 99%

“… Glucose metabolism Voss et al 18 KIF3A KIF3A-N-Cadherin Cell adhesion Phang et al 19 KIF3A KIF3A-N-Cadherin and PAR3/Cdc42 Cell polarity Hoon et al 20 Pcdh-γC5 Pcdh-γC5-CAMKII Endogenous activator of POPX2 Onouchi et al 21 Neurofilament L ? Neurofilament L-mediated filament assembly Ozaki et al 22 TAK1 TAK1-IKK-NF-kB Apoptosis Weng and Koh 15 LATS1 MST-LATS-YAP/TAZ Anchorage-dependent growth Rahmat et al 12 Chk1 ATM/ATR-Chk1 Cell-cycle progression Kim et al 23 …”

Section: The Binding Partners Of Popx2mentioning

confidence: 99%

Partners in crime: POPX2 phosphatase and its interacting proteins in cancer

Kim¹,

Zhang²,

Rahmat³

et al. 2020

Cell Death Dis

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Protein phosphorylation and dephosphorylation govern intracellular signal transduction and cellular functions. Kinases and phosphatases are involved in the regulation and development of many diseases such as Alzheimer’s, diabetes, and cancer. While the functions and roles of many kinases, as well as their substrates, are well understood, phosphatases are comparatively less well studied. Recent studies have shown that rather than acting on fewer and more distinct substrates like the kinases, phosphatases can recognize specific phosphorylation sites on many different proteins, making the study of phosphatases and their substrates challenging. One approach to understand the biological functions of phosphatases is through understanding their protein–protein interaction network. POPX2 (Partner of PIX 2; also known as PPM1F or CaMKP) is a serine/threonine phosphatase that belongs to the PP2C family. It has been implicated in cancer cell motility and invasiveness. This review aims to summarize the different binding partners of POPX2 phosphatase and explore the various functions of POPX2 through its interactome in the cell. In particular, we focus on the impact of POPX2 on cancer progression. Acting via its different substrates and interacting proteins, POPX2’s involvement in metastasis is multifaceted and varied according to the stages of metastasis.

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Ca 2+ /calmodulin-dependent protein kinase phosphatase (CaMKP/PPM1F) interacts with neurofilament L and inhibits its filament association

Cited by 7 publications

References 22 publications

Loss of PPM1F expression predicts tumour recurrence and is negatively regulated by miR‐590‐3p in gastric cancer

Loss of PPM1F expression predicts tumour recurrence and is negatively regulated by miR‐590‐3p in gastric cancer

PPM1F regulates ovarian cancer progression by affecting the dephosphorylation of ITGB1

Partners in crime: POPX2 phosphatase and its interacting proteins in cancer

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