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Article ; Online: PP2A Affects Angiogenesis via Its Interaction with a Novel Phosphorylation Site of TSP1.

Thalwieser, Zsófia / Fonódi, Márton / Király, Nikolett / Csortos, Csilla / Boratkó, Anita

International journal of molecular sciences

2024 Volume 25, Issue 3

Abstract: Alterations in angiogenic properties play a pivotal role in the manifestation and onset of various pathologies, including vascular diseases and cancer. Thrombospondin-1 (TSP1) protein is one of the master regulators of angiogenesis. This study unveils a ... ...

Abstract	Alterations in angiogenic properties play a pivotal role in the manifestation and onset of various pathologies, including vascular diseases and cancer. Thrombospondin-1 (TSP1) protein is one of the master regulators of angiogenesis. This study unveils a novel aspect of TSP1 regulation through reversible phosphorylation. The silencing of the B55α regulatory subunit of protein phosphatase 2A (PP2A) in endothelial cells led to a significant decrease in TSP1 expression. Direct interaction between TSP1 and PP2A-B55α was confirmed via various methods. Truncated TSP1 constructs were employed to identify the phosphorylation site and the responsible kinase, ultimately pinpointing PKC as the enzyme phosphorylating TSP1 on Ser93. The biological effects of B55α-TSP1 interaction were also analyzed. B55α silencing not only counteracted the increase in TSP1 expression during wound closure but also prolonged wound closure time. Although B55α silenced cells initiated tube-like structures earlier than control cells, their spheroid formation was disrupted, leading to disintegration. Cells transfected with phosphomimic TSP1 S93D exhibited smaller spheroids and reduced effectiveness in tube formation, revealing insights into the effects of TSP1 phosphorylation on angiogenic properties. In this paper, we introduce a new regulatory mechanism of angiogenesis by reversible phosphorylation on TSP1 S93 by PKC and PP2A B55α.
MeSH term(s)	Angiogenesis ; Endothelial Cells/metabolism ; Phosphorylation ; Protein Phosphatase 2/metabolism ; Protein Processing, Post-Translational ; Thrombospondin 1/genetics ; Thrombospondin 1/metabolism ; Humans
Chemical Substances	Protein Phosphatase 2 (EC 3.1.3.16) ; Thrombospondin 1
Language	English
Publishing date	2024-02-03
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms25031844
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Article ; Online: TIMAP, a Regulatory Subunit of Protein Phosphatase 1, Inhibits In Vitro Neuronal Differentiation.

Fonódi, Márton / Thalwieser, Zsófia / Csortos, Csilla / Boratkó, Anita

International journal of molecular sciences

2023 Volume 24, Issue 24

Abstract: TIMAP (TGF-β-inhibited membrane associated protein) is abundant in endothelial cells, and it has been regarded as a member of the myosin phosphatase targeting protein (MYPT) family. Our workgroup previously identified several interacting protein partners ...

Abstract	TIMAP (TGF-β-inhibited membrane associated protein) is abundant in endothelial cells, and it has been regarded as a member of the myosin phosphatase targeting protein (MYPT) family. Our workgroup previously identified several interacting protein partners of TIMAP and proved its regulatory subunit role for protein phosphatase 1 catalytic subunit (PP1c). TIMAP is also expressed in neuronal cells, but details of its function have not been studied yet. Therefore, we aimed to explore the role of TIMAP in neuronal cells, especially during differentiation. Expression of TIMAP was proved both at mRNA and protein levels in SH-SY5Y human neuroblastoma cells. Differentiation of SH-SY5Y cells was optimized and proved by the detection of neuronal differentiation markers, such as β3-tubulin, nestin and inhibitor of differentiation 1 (ID1) using qPCR and Western blot. We found downregulation of TIMAP during differentiation. In accordance with this, overexpression of recombinant TIMAP attenuated the differentiation of neuronal cells. Moreover, the subcellular localization of TIMAP has changed during differentiation as it translocated from the plasma membrane into the nucleus. The nuclear interactome of TIMAP revealed more than 50 proteins, offering the possibility to further investigate the role of TIMAP in several key physiological pathways of neuronal cells.
MeSH term(s)	Humans ; Cell Differentiation ; Endothelial Cells/metabolism ; Membrane Proteins/metabolism ; Neuroblastoma/metabolism ; Protein Phosphatase 1/metabolism ; Protein Processing, Post-Translational ; Neurons/cytology
Chemical Substances	Membrane Proteins ; Protein Phosphatase 1 (EC 3.1.3.16) ; PPP1R16B protein, human
Language	English
Publishing date	2023-12-11
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms242417360
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Article ; Online: TIMAP, a Regulatory Subunit of Protein Phosphatase 1, Inhibits In Vitro Neuronal Differentiation

Márton Fonódi / Zsófia Thalwieser / Csilla Csortos / Anita Boratkó

International Journal of Molecular Sciences, Vol 24, Iss 24, p

2023 Volume 17360

Abstract	TIMAP (TGF-β-inhibited membrane associated protein) is abundant in endothelial cells, and it has been regarded as a member of the myosin phosphatase targeting protein (MYPT) family. Our workgroup previously identified several interacting protein partners of TIMAP and proved its regulatory subunit role for protein phosphatase 1 catalytic subunit (PP1c). TIMAP is also expressed in neuronal cells, but details of its function have not been studied yet. Therefore, we aimed to explore the role of TIMAP in neuronal cells, especially during differentiation. Expression of TIMAP was proved both at mRNA and protein levels in SH-SY5Y human neuroblastoma cells. Differentiation of SH-SY5Y cells was optimized and proved by the detection of neuronal differentiation markers, such as β3-tubulin, nestin and inhibitor of differentiation 1 (ID1) using qPCR and Western blot. We found downregulation of TIMAP during differentiation. In accordance with this, overexpression of recombinant TIMAP attenuated the differentiation of neuronal cells. Moreover, the subcellular localization of TIMAP has changed during differentiation as it translocated from the plasma membrane into the nucleus. The nuclear interactome of TIMAP revealed more than 50 proteins, offering the possibility to further investigate the role of TIMAP in several key physiological pathways of neuronal cells.
Keywords	TIMAP ; protein phosphatase ; neuroblastoma ; differentiation ; interactome ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	570
Language	English
Publishing date	2023-12-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: Ser69 phosphorylation of TIMAP affects endothelial cell migration.

Király, Nikolett / Csortos, Csilla / Boratkó, Anita

Experimental lung research

2021 Volume 47, Issue 7, Page(s) 334–343

Abstract: Purpose/aim: TIMAP (TGF-β-inhibited membrane-associated protein) is a regulatory subunit of protein phosphatase 1 (PP1). The N-terminal region contains a binding motif for the catalytic subunit of PP1 (PP1c) and a nuclear localization signal (NLS). ... ...

Abstract	Purpose/aim: TIMAP (TGF-β-inhibited membrane-associated protein) is a regulatory subunit of protein phosphatase 1 (PP1). The N-terminal region contains a binding motif for the catalytic subunit of PP1 (PP1c) and a nuclear localization signal (NLS). Phosphorylation of TIMAP on Ser331, Ser333 and Ser337 side chains was shown to regulate the activity of the TIMAP-PP1c complex. Several studies, however, reported an additional side chain of TIMAP. Ser69 is located near to the PP1c binding motif and NLS, therefore, we hypothesized that the phosphorylation of this side chain perhaps may regulate the interaction between TIMAP and PP1c, or may affect the nuclear transport of TIMAP.
MeSH term(s)	Cell Movement ; Endothelial Cells/metabolism ; Membrane Proteins/metabolism ; Phosphorylation ; Protein Phosphatase 1/metabolism
Chemical Substances	Membrane Proteins ; Protein Phosphatase 1 (EC 3.1.3.16)
Language	English
Publishing date	2021-08-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	603791-4
ISSN	1521-0499 ; 0190-2148
ISSN (online)	1521-0499
ISSN	0190-2148
DOI	10.1080/01902148.2021.1960651
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Article ; Online: Dephosphorylation of annexin A2 by protein phosphatase 1 regulates endothelial cell barrier.

Király, Nikolett / Thalwieser, Zsófia / Fonódi, Márton / Csortos, Csilla / Boratkó, Anita

IUBMB life

2021 Volume 73, Issue 10, Page(s) 1257–1268

Abstract: Annexin A2 (ANXA2) is a multifunctional protein expressed in nearly all human tissues and cell types, playing a role in various signaling pathways. It is subjected to phosphorylation, but no specific protein phosphatase has been identified in its ... ...

Abstract	Annexin A2 (ANXA2) is a multifunctional protein expressed in nearly all human tissues and cell types, playing a role in various signaling pathways. It is subjected to phosphorylation, but no specific protein phosphatase has been identified in its posttranslational regulation yet. Using pull-down assay followed by liquid chromatography-mass spectrometry analysis we found that ANXA2 interacts with TIMAP (TGF-beta-inhibited membrane-associated protein) in pulmonary artery endothelial cells. TIMAP is highly expressed in endothelial cells, where it acts as a regulatory and targeting subunit of protein phosphatase 1 (PP1). TIMAP plays an important role in the regulation of the endothelial barrier maintenance through the dephosphorylation of its several substrate proteins. In the present work, phosphorylation of Ser25 side chain in ANXA2 by protein kinase C (PKC) was shown both in vivo and in vitro. Phosphorylation level of ANXA2 at Ser25 increased greatly by inhibition of PP1 and by depletion of its regulatory subunit, TIMAP, implying a role of this PP1 holoenzyme in the dephosphorylation of ANXA2. Immunofluorescence staining and subcellular fractionations revealed a diffuse subcellular localization for the endogenous ANXA2, but phospho-Ser25 ANXA2 was mainly detected in the membrane. ANXA2 depletion lowered the basal endothelial barrier and inhibited cell migration, but had no significant effect on cell proliferation or viability. ANXA2 depleted cells failed to respond to PMA treatment, indicating an intimately involvement of phospho-ANXA2 in PKC signaling. Moreover, phosphorylation of ANXA2 disrupted its interaction with S100A10 suggesting a phosphorylation dependent multiple regulatory role of ANXA2 in endothelial cells. Our results demonstrate the pivotal role of PKC-ANXA2-PP1 pathway in endothelial cell signaling, especially in barrier function and cell migration.
MeSH term(s)	Animals ; Annexin A2/genetics ; Annexin A2/metabolism ; Cattle ; Cell Movement ; Cells, Cultured ; Endothelial Cells/metabolism ; Endothelium, Vascular/cytology ; Endothelium, Vascular/physiology ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Phosphorylation ; Protein Interaction Domains and Motifs ; Protein Kinase C/metabolism ; Protein Phosphatase 1/metabolism ; Pulmonary Artery/cytology ; Serine/metabolism
Chemical Substances	ANXA2 protein, human ; Annexin A2 ; Membrane Proteins ; PPP1R16B protein, human ; Serine (452VLY9402) ; Protein Kinase C (EC 2.7.11.13) ; Protein Phosphatase 1 (EC 3.1.3.16)
Language	English
Publishing date	2021-08-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1492141-8
ISSN	1521-6551 ; 1521-6543
ISSN (online)	1521-6551
ISSN	1521-6543
DOI	10.1002/iub.2538
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Zs.A 1611: Show issues

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Article ; Online: TIMAP, the versatile protein phosphatase 1 regulator in endothelial cells.

Boratkó, Anita / Csortos, Csilla

IUBMB life

2017 Volume 69, Issue 12, Page(s) 918–928

Abstract: Transforming growth factor (TGF)-β inhibited membrane associated protein, TIMAP, is the member of the myosin phosphatase targeting protein (MYPT) family of protein phosphatase 1 (PP1) regulatory subunits. The N-terminal part of TIMAP has a typical MYPT ... ...

Abstract	Transforming growth factor (TGF)-β inhibited membrane associated protein, TIMAP, is the member of the myosin phosphatase targeting protein (MYPT) family of protein phosphatase 1 (PP1) regulatory subunits. The N-terminal part of TIMAP has a typical MYPT family structure with a sequence element called MyPhone (myosin phosphatase N-terminal element), a putative bipartite nuclear localization signal, a PP1 catalytic subunit binding motif, and five ankyrin repeats. The C-terminal half of TIMAP is intrinsically disordered, but ends with a functional CAAX box for lipid modification which allows localization of TIMAP at the plasma membrane. TIMAP is prenylated by farnesyl transferase with the contribution of the anchoring protein, RACK1 in the cytoplasm. The controlling effect of TIMAP on PP1 is moderated by PKA/GSK3β and PKC mediated phosphorylation of TIMAP, the sites are located in the disordered region of the protein. TIMAP is abundant in endothelial cells. A growing body of evidence attained through characterization of newly identified protein partners calls attention to its critical role in normal and pathological activities of the endothelium via regulation of PP1. TIMAP binds the non-integrin laminin receptor 1 and the endothelin converting enzyme 1, which may connect TIMAP to angiogenesis, tumor invasion and metastasis. Barrier protecting role of TIMAP was shown for pulmonary artery endothelial cells. ERM (ezrin-radixin-moesin) proteins, as potential in vivo PP1-TIMAP substrates, are critical targets in the barrier maintenance. TIMAP affects phosphorylation level and subcellular localization of merlin and eukaryotic elongation factor-1A1. Merlin is a key component of signaling pathways regulating cell proliferation, membrane domain formation and cell-cell junction organization. Noncanonical functions of the elongation factor include a role in organization of cytoskeleton dynamics and in apoptosis. The interacting/binding partners identified so far demonstrate a rather complex role of TIMAP in key functions of the endothelium offering TIMAP as a plausible target in pathological issues. © 2017 IUBMB Life, 69(12):918-928, 2017.
MeSH term(s)	Animals ; Conserved Sequence ; Cyclic AMP-Dependent Protein Kinases/genetics ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Endothelial Cells/cytology ; Endothelial Cells/metabolism ; GTP Phosphohydrolases/genetics ; GTP Phosphohydrolases/metabolism ; Gene Expression Regulation ; Glycogen Synthase Kinase 3 beta/genetics ; Glycogen Synthase Kinase 3 beta/metabolism ; Humans ; Hypertension/genetics ; Hypertension/metabolism ; Hypertension/pathology ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Neoplasms/genetics ; Neoplasms/metabolism ; Neoplasms/pathology ; Neurofibromin 2/genetics ; Neurofibromin 2/metabolism ; Protein Binding ; Protein Phosphatase 1/genetics ; Protein Phosphatase 1/metabolism ; Receptors for Activated C Kinase/genetics ; Receptors for Activated C Kinase/metabolism ; Signal Transduction ; Stroke/genetics ; Stroke/metabolism ; Stroke/pathology
Chemical Substances	EFL1 protein, human ; Membrane Proteins ; Neoplasm Proteins ; Neurofibromin 2 ; PPP1R16B protein, human ; RACK1 protein, human ; Receptors for Activated C Kinase ; Glycogen Synthase Kinase 3 beta (EC 2.7.11.1) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11) ; Protein Phosphatase 1 (EC 3.1.3.16) ; GTP Phosphohydrolases (EC 3.6.1.-)
Language	English
Publishing date	2017-11-15
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1492141-8
ISSN	1521-6551 ; 1521-6543
ISSN (online)	1521-6551
ISSN	1521-6543
DOI	10.1002/iub.1695
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Article: PKC mediated phosphorylation of TIMAP regulates PP1c activity and endothelial barrier function.

Boratkó, Anita / Csortos, Csilla

Biochimica et biophysica acta. Molecular cell research

2016 Volume 1864, Issue 2, Page(s) 431–439

Abstract: TGF-β inhibited membrane-associated protein (TIMAP) is greatly expressed in endothelial cell lines and serves as a protein phosphatase 1 (PP1) regulatory subunit. Phosphorylation state of TIMAP, through affecting PP1 activity, has a remarkable effect on ... ...

Abstract	TGF-β inhibited membrane-associated protein (TIMAP) is greatly expressed in endothelial cell lines and serves as a protein phosphatase 1 (PP1) regulatory subunit. Phosphorylation state of TIMAP, through affecting PP1 activity, has a remarkable effect on endothelial barrier function. Here we present evidence for a previously unidentified PKC phosphorylation site in TIMAP. Protein-protein interaction was detected in pulmonary endothelial cells between endogenous TIMAP and activated PKCα. PKCα phosphorylated the full length recombinant TIMAP in in vitro kinase assay and Ser331 of TIMAP was shown to be phosphorylated by PKC. Phosphorylation of TIMAP upon PKC activation in endothelial cells results in enrichment of TIMAP in the membrane, but no such change can be observed in PKC depleted cells. However, the previously identified PKA/GSK-3β induced enrichment of TIMAP at the plasma membrane was not affected in the absence of PKC. Interaction between TIMAP and the TIMAP-PP1 substrate phospho-ERM was described earlier, but now we show that binding of PKC phosphorylated TIMAP to ERM is severely reduced. This suggests an inhibitory effect of phospho-Ser331 on TIMAP-PP1 activity toward phospho-ERM. Accordingly, phospho-ERM level in the membrane fraction of the phospho-mimic S331D TIMAP mutant transfected cells was increased, but the S331A mutant overexpressing endothelial cells had a lower phospho-ERM level. Consistent with the phospho-ERM level, electric resistance measurements showed that the S331A mutation of TIMAP resulted in faster recovery from the PMA treatment. Taken together, phosphorylation of TIMAP on Ser331 by PKC represents a new mechanism of endothelial barrier regulation, through the inhibition of phospho-ERM dephosphorylation.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cells, Cultured ; Endothelium, Vascular/cytology ; Endothelium, Vascular/physiology ; Glycogen Synthase Kinase 3 beta/metabolism ; Humans ; Membrane Proteins/metabolism ; Phosphorylation ; Protein Kinase C-alpha/metabolism ; Protein Phosphatase 1/chemistry ; Protein Phosphatase 1/metabolism ; Protein Transport ; Sequence Homology, Amino Acid ; Substrate Specificity
Chemical Substances	Membrane Proteins ; PPP1R16B protein, human ; Glycogen Synthase Kinase 3 beta (EC 2.7.11.1) ; Protein Kinase C-alpha (EC 2.7.11.13) ; Protein Phosphatase 1 (EC 3.1.3.16)
Language	English
Publishing date	2016-12-06
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0167-4889 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0167-4889 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2016.12.001
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Article ; Online: Protein phosphatase 2A-mediated flotillin-1 dephosphorylation up-regulates endothelial cell migration and angiogenesis regulation.

Thalwieser, Zsófia / Király, Nikolett / Fonódi, Márton / Csortos, Csilla / Boratkó, Anita

The Journal of biological chemistry

2019 Volume 294, Issue 52, Page(s) 20196–20206

Abstract: Endothelial cells have key functions in endothelial barrier integrity and in responses to angiogenic signals that promote cell proliferation, cell migration, cytoskeletal reorganization, and formation of new blood vessels. These functions highly depend ... ...

Abstract	Endothelial cells have key functions in endothelial barrier integrity and in responses to angiogenic signals that promote cell proliferation, cell migration, cytoskeletal reorganization, and formation of new blood vessels. These functions highly depend on protein-protein interactions in cell-cell junction and cell attachment complexes and on interactions with cytoskeletal proteins. Protein phosphatase 2A (PP2A) dephosphorylates several target proteins involved in cytoskeletal dynamics and cell adhesion. Our goal was to find new interacting and substrate proteins of the PP2A-B55α holoenzyme in bovine pulmonary endothelial cells. Using LC-MS/MS analysis, we identified flotillin-1 as a protein that binds recombinant GSH
MeSH term(s)	Animals ; Carbazoles/pharmacology ; Cattle ; Cell Movement ; Cells, Cultured ; Endothelial Cells/cytology ; Endothelial Cells/metabolism ; Holoenzymes/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mutagenesis, Site-Directed ; Neovascularization, Physiologic ; Phosphorylation/drug effects ; Protein Interaction Domains and Motifs ; Protein Kinase C/metabolism ; Protein Phosphatase 2/antagonists & inhibitors ; Protein Phosphatase 2/genetics ; Protein Phosphatase 2/metabolism ; Protein Subunits/genetics ; Protein Subunits/metabolism ; RNA Interference ; RNA, Small Interfering/metabolism ; Up-Regulation
Chemical Substances	Carbazoles ; Holoenzymes ; Membrane Proteins ; Protein Subunits ; RNA, Small Interfering ; flotillins ; Go 6976 (136194-77-9) ; Protein Kinase C (EC 2.7.11.13) ; Protein Phosphatase 2 (EC 3.1.3.16)
Language	English
Publishing date	2019-11-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA119.007980
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Article ; Online: Regulation of merlin by protein phosphatase 1-TIMAP and EBP50 in endothelial cells.

Boratkó, Anita / Péter, Margit / Csortos, Csilla

The international journal of biochemistry & cell biology

2017 Volume 82, Page(s) 10–17

Abstract: Merlin (moesin-ezrin-radixin like protein), the product of neurofibromatosis type 2 gene, was primarily recognized as a tumor suppressor, but it also functions as a membrane-cytoskeletal linker and regulator of multiple signaling pathways. The activity ... ...

Abstract	Merlin (moesin-ezrin-radixin like protein), the product of neurofibromatosis type 2 gene, was primarily recognized as a tumor suppressor, but it also functions as a membrane-cytoskeletal linker and regulator of multiple signaling pathways. The activity and localization of merlin is regulated by head to tail folding that is controlled by phosphorylation of the Ser518 side chain. Merlin localizes in the nucleus when the Ser518 side chain is not phosphorylated, while the phosphorylated form is present in the cytoplasm and the plasma membrane. In this work interactions and their impact on the subcellular localization and phosphorylation state of the Ser518 side chain of merlin were investigated in endothelial cells. It is shown that merlin (dephospho-Ser518 form) interacts in the nucleus of endothelial cells with the scaffolding protein EBP50, a member of the Na
MeSH term(s)	Active Transport, Cell Nucleus ; Animals ; Cattle ; Cells, Cultured ; Endothelium, Vascular/cytology ; Endothelium, Vascular/metabolism ; Humans ; Membrane Proteins/antagonists & inhibitors ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mutation ; Neurofibromin 2/chemistry ; Neurofibromin 2/genetics ; Neurofibromin 2/metabolism ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Phosphoproteins/antagonists & inhibitors ; Phosphoproteins/chemistry ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Interaction Mapping ; Protein Multimerization ; Protein Processing, Post-Translational ; Pulmonary Artery/cytology ; RNA Interference ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Serine/metabolism ; Sodium-Hydrogen Exchangers/antagonists & inhibitors ; Sodium-Hydrogen Exchangers/chemistry ; Sodium-Hydrogen Exchangers/genetics ; Sodium-Hydrogen Exchangers/metabolism
Chemical Substances	Membrane Proteins ; Neurofibromin 2 ; PPP1R16B protein, human ; Peptide Fragments ; Phosphoproteins ; Recombinant Fusion Proteins ; Recombinant Proteins ; Sodium-Hydrogen Exchangers ; sodium-hydrogen exchanger regulatory factor ; Serine (452VLY9402)
Language	English
Publishing date	2017-01
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1228429-4
ISSN	1878-5875 ; 1357-2725
ISSN (online)	1878-5875
ISSN	1357-2725
DOI	10.1016/j.biocel.2016.11.010
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Article ; Online: NHERF2 is crucial in ERM phosphorylation in pulmonary endothelial cells.

Boratkó, Anita / Csortos, Csilla

Cell communication and signaling : CCS

2013 Volume 11, Page(s) 99

Abstract: Background: EBP50 and NHERF2 adaptor proteins are incriminated in various signaling pathways of the cell. They can bind ERM proteins and mediate ERM-membrane protein interactions.: Results: Binding of ERM to EBP50 and NHERF2 was compared in pulmonary ...

Abstract	Background: EBP50 and NHERF2 adaptor proteins are incriminated in various signaling pathways of the cell. They can bind ERM proteins and mediate ERM-membrane protein interactions. Results: Binding of ERM to EBP50 and NHERF2 was compared in pulmonary artery endothelial cells by immunoprecipitation. NHERF2 associates with all three ERM, but EBP50 appeared to be a weak binding partner if at all. Furthermore, we detected co-localization of NHERF2 and phospho-ERM at the cell membrane and in the filopodia of dividing cells. Silencing of NHERF2 prevented agonist or angiogenesis induced phosphorylation of ERM, while overexpression of the adaptor elevated the phosphorylation level of ERM, likely catalyzed by Rho kinase 2, which co-immunoprecipitated with NHERF2/ERM in control EC, but did not bind to ERM in NHERF2 depleted cells. Dependence of ERM phosphorylation on NHERF2 was also shown in Matrigel tube formation assay, and NHERF2 was proved to be important in angiogenesis as well. Furthermore, when NHERF2 was depleted or cells were overexpressing a mutant form of NHERF2 unable to bind ERM, we found attenuated cell attachment with ECIS measurements, while it was supported by overexpression of wild type NHERF2. Conclusions: Pivotal role of NHERF2 in the phosphorylation process of ERM in pulmonary artery endothelial cells is shown. We propose that NHERF2 provides a common anchoring surface for ERM and Rho kinase 2. Our results demonstrate the essential role of NHERF2 in endothelial cell adhesion/migration and angiogenesis.
MeSH term(s)	Animals ; Cattle ; Cytoskeletal Proteins/genetics ; Cytoskeletal Proteins/metabolism ; Endothelial Cells/metabolism ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Neovascularization, Physiologic ; Neurofibromin 2/genetics ; Neurofibromin 2/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Structure, Tertiary ; Pseudopodia/metabolism ; Pulmonary Artery/metabolism ; Sodium-Hydrogen Exchangers/metabolism ; rho-Associated Kinases/metabolism
Chemical Substances	Cytoskeletal Proteins ; Membrane Proteins ; Microfilament Proteins ; Neurofibromin 2 ; Phosphoproteins ; Sodium-Hydrogen Exchangers ; ezrin ; sodium-hydrogen exchanger regulatory factor ; moesin (144131-77-1) ; radixin (144517-21-5) ; rho-Associated Kinases (EC 2.7.11.1)
Language	English
Publishing date	2013-12-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1478-811X
ISSN (online)	1478-811X
DOI	10.1186/1478-811X-11-99
Database	MEDical Literature Analysis and Retrieval System OnLINE

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