14-kDa phosphohistidine phosphatase and its role in human lung cancer cell migration and invasion

Xu, Anjian; Hao, Jia; Zhang, Zhao; Tian, Tian; Jiang, Sanyi; Hao, Juanting; Liu, Chuanjun; Huang, Lingyun; Xiao, Xueyuan; He, Dacheng

doi:10.1016/j.lungcan.2009.03.005

Cited by 42 publications

(49 citation statements)

References 28 publications

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“…28 In this particular case, it is not clear which isomer of pHis is formed and on which His residue. Mammalian pHis phosphatases, which have been characterized include: protein pHis phosphatase 1 (PHPT1); 17,[29][30][31][32][33][34][35] Lys/His phosphatase (LHPPase); 36,37 Ser Thr protein phosphatases (PP1/2 A/2C); 38,39 T-cell ubiquitin ligand-2 (TULA-2); 40,41 and the recently reported phosphoglycerate mutase-5 (PGAM5). 42 In addition, pHis phosphatase activity has been reported in rat tissue extracts but these have not been fully characterized.…”

mentioning

confidence: 99%

Advances in development of new tools for the study of phosphohistidine

Makwana

Muimo

Jackson

2018

Laboratory Investigation

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Protein phosphorylation is an important post-translational modification that is an integral part of cellular function. The O-phosphorylated amino-acid residues, such as phosphoserine (pSer), phosphothreonine (pThr) and phosphotyrosine (pTyr), have dominated the literature while the acid labile N-linked phosphorylated amino acids, such as phosphohistidine (pHis), have largely been historically overlooked because of the acidic conditions routinely used in amino-acid detection and analysis. This review highlights some misinterpretations that have arisen in the existing literature, pinpoints outstanding questions and potential future directions to clarify the role of pHis in mammalian signalling systems. Particular emphasis is placed on pHis isomerization and the hybrid functionality for both pHis and pTyr of the proposed τ-pHis analogue bearing the triazole residue.

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mentioning

confidence: 99%

Advances in development of new tools for the study of phosphohistidine

Makwana

Muimo

Jackson

2018

Laboratory Investigation

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“…Phosphohistidine phosphatase (PHP14) was proposed to be another lung cancer prognostic biomarker, regulating cell migration and invasion by cytoskeleton rearrangement. Indeed, it has been shown that PHP14 knockdown in highly metastatic lung cancer cells (CL1-5) inhibited migration and invasion, whereas its over-expression in NCI H1299 cells enhanced these processes (67). Calmodulin, a protein implicated in cytoskeletal alterations during cell death, thymosin 4, a regulator of actin polymerization whose over-expression seems to stimulate lung tumour metastasis, thymosin 10 and cofilin proteins, regulators of actin dynamics, were identified and their expression and prognostic role validated on cohort of 188 lung cancer cases (68).…”

Section: Prognostic Biomarkersmentioning

confidence: 99%

Oncoproteomic Approaches in Lung Cancer Research

Pastor¹,

Nogal²,

Molina-Pinelo³

et al. 2013

Oncogenomics and Cancer Proteomics - Novel Approaches in Biomarkers Discovery and Therapeutic Targets in Cancer

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“…Recent studies by Xu et al (44) have suggested that the 14-kDa PHP might be involved in lung cancer cell migration and invasion of lung cancer cells through the regulation of actin cytoskeletal rearrangements. Therefore, as a logical extension to the studies described under Fig.…”

Section: Php Does Not Mediate Glucose-induced Activation Of Rac1 In Imentioning

confidence: 99%

Regulation of glucose- and mitochondrial fuel-induced insulin secretion by a cytosolic protein histidine phosphatase in pancreatic β-cells

Kamath

Kyathanahalli

Jayaram

et al. 2010

American Journal of Physiology-Endocrinology and Metabolism

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localization of a cytosolic protein histidine phosphatase (PHP; ϳ16 kDa) in INS 832/13 cells, normal rat islets, and human islets. siRNA-mediated knockdown of PHP markedly reduced glucose-or mitochondrial fuel-induced but not KCl-induced insulin secretion. siRNA-mediated knockdown of PHP also attenuated mastoparan-induced insulin secretion, suggesting its participation in G protein-sensitive signaling steps, leading to insulin secretion. Functional assays revealed that the ␤-cell PHP catalyzes the dephosphorylation of ATP-citrate lyase (ACL). Silencing of PHP expression markedly reduced ACL activity, suggesting functional regulation of ACL by PHP in ␤-cells. Coimmunoprecipitation studies revealed modest effects of glucose on the interaction between PHP and ACL. Confocal microscopic evidence indicated that glucose promotes association between ACL and nm23-H1, a known kinase histidine kinase, but not between PHP and ACL. Furthermore, metabolic viability of INS 832/13 cells was resistant to siRNA-PHP, suggesting no regulatory roles of PHP in cell viability. Finally, long-term exposure (24 h) of INS 832/13 cells or rat islets to high glucose (30 mM) increased the expression of PHP. Such increases in PHP expression were also seen in islets derived from the Zucker diabetic fatty rat compared with islets from the lean control animals. Together, these data implicate regulatory roles for PHP in a G protein-sensitive step involved in nutrient-induced insulin secretion. In light of the current debate on putative regulatory roles of ACL in insulin secretion, additional studies are needed to precisely identify the phosphoprotein substrate(s) for PHP in the cascade of events leading to nutrient-induced insulin secretion. nm23-H1; adenosine 5=-triphosphate-citrate lyase IT IS WELL ESTABLISHED THAT in the majority of cell types transduction of extracellular signals involves ligand binding to a receptor, often followed by the activation of one or more GTP-binding proteins (G proteins) and their effector systems (7). The pancreatic ␤-cell is unusual in that glucose, the major physiological agonist, lacks an extracellular receptor. Instead, events consequent to glucose metabolism promote insulin secretion via the generation and/or altered distribution of diffusible second messengers such as calcium, cAMP, and lipid hydrolytic products of various phospholipases (5,28,32,34,36). It is noteworthy that a selective increase in intracellular calcium not only initiates insulin secretion but also regulates various enzymes such as protein kinases, phosphodiesterases, adenylyl cyclases, and phospholipases, thereby facilitating insulin secretion. In the context of protein kinases, in addition to calcium-dependent protein kinase(s), several other kinases, including calmodulin-, cyclic nucleotide-, and phospholipiddependent protein kinases, tyrosine kinases, and mitogen-

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14-kDa phosphohistidine phosphatase and its role in human lung cancer cell migration and invasion

Cited by 42 publications

References 28 publications

Advances in development of new tools for the study of phosphohistidine

Advances in development of new tools for the study of phosphohistidine

Oncoproteomic Approaches in Lung Cancer Research

Regulation of glucose- and mitochondrial fuel-induced insulin secretion by a cytosolic protein histidine phosphatase in pancreatic β-cells

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