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1.

001-es BibID:BIBFORM028724
Első szerző:Erdődi Ferenc (biokémikus)
Cím:Phosphorylation of protein phosphatase type-1 inhibitory proteins by integrin-linked kinase and cyclic nucleotide-dependent protein kinases / Ferenc Erdődi, Enikő Kiss, Michael P. Walsh, Bjarki Stefansson, Jing Ti Deng, Masumi Eto, David L. Brautigan, David J. Hartshorne
Dátum:2003
ISSN:0006-291X
Megjegyzések:Protein phosphatases play key roles in cellular regulation and are subjected to control by protein inhibitors whose activity is in turn regulated by phosphorylation. Here we investigated the possible regulation of phosphorylation-dependent type-1 protein phosphatase (PP1) inhibitors, CPI-17, PHI-1, and KEPI, by various kinases. Protein kinases A (PKA) and G (PKG) phosphorylated CPI-17 at the inhibitory site (T38), but not PHI-1 (T57). Phosphorylated CPI-17 inhibited the activity of both the PP1 catalytic subunit (PP1c) and the myosin phosphatase holoenzyme (MPH) with IC(50) values of 1-8 nM. PKA predominantly phosphorylated a site distinct from the inhibitory T73 in KEPI, whereas PKG was ineffective. Integrin-linked kinase phosphorylated KEPI (T73) and this dramatically increased inhibition of PP1c (IC(50)=0.1 nM) and MPH (IC(50)=8 nM). These results suggest that the regulatory phosphorylation of CPI-17 and KEPI may involve distinct kinases and signaling pathways.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
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Megjelenés:Biochemical and Biophysical Research Communications. - 306 : 2 (2003), p. 382-387. -
További szerzők:Kiss Enikő Walsh, Michael P. Stefansson, Bjarki Deng, Jing Ti Eto, Masumi Brautigan, David L. Hartshorne, David J.
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2.

001-es BibID:BIBFORM029379
Első szerző:Kiss Enikő
Cím:The role of subunit interactions and phosphorylation in the regulation of myosin phosphatase / Enikő Kiss, Attila Tóth, Ferenc Erdődi
Dátum:2001
ISBN:1586031805
Tárgyszavak:Orvostudományok Elméleti orvostudományok előadáskivonat
egyetemen (Magyarországon) készült közlemény
Megjelenés:NATO science series, Series A. Life sciences / eds. L. Heilmeyer, P. Friedrich. - p. 232-240.
További szerzők:Erdődi Ferenc (1953-) (biokémikus) Tóth Attila (orvos) Protein Modules in Cellular Signaling : Proceedings of the NATO Advanced Study Institute on Protein Modules in Cellular Signalling (1) (2000) (St Martin de Londres, Franciaország)
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3.

001-es BibID:BIBFORM028726
Első szerző:Kiss Enikő
Cím:Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton / Enikő Kiss, Andrea Murányi, Csilla Csortos, Pál Gergely, Masaaki Ito, David J. Hartshorne, Ferenc Erdődi
Dátum:2002
ISSN:0264-6021
Megjegyzések:The myosin phosphatase (MP) composed of the catalytic subunit of type 1 protein phosphatase and myosin phosphatase target subunit isoform 1 (MYPT1) was identified as the major serine/threonine phosphatase component in the platelet-cytoskeleton fraction. MYPT1 was phosphorylated by cytoskeletal kinase(s), but the identity of the kinase(s) and the effect of phosphorylation were not established. Incubation of platelet-cytoskeletal fraction with MgATP or MgATP[S] (magnesium adenosine 5'-[gamma-thio]triphosphate) caused a decrease in the 20 kDa light-chain of smooth-muscle myosin (MLC20) phosphatase and phosphorylase phosphatase activities. MYPT1 contains a phosphorylation site, Thr-695, involved in the inhibition of MP in a RhoA/Rho kinase-dependent manner. The cytoskeletal kinase(s) phosphorylated Thr-695 of glutathione S-transferase (GST)-MYPT1, as determined with an antibody specific for phosphorylated Thr-695. The level of Rho kinase was low in the cytoskeletal fraction and was detected primarily in the membrane and cytosolic fractions. The phosphorylation of Thr-695 by the cytoskeletal kinase(s) was not affected by Rho kinase inhibitor, Y-27632, suggesting that kinase(s) other than Rho kinase were involved. In-gel kinase assay identified a kinase at 54-59 kDa that phosphorylated the C-terminal fragment of MYPT1 (GST-MYPT1(667-1004)). Western blots detected both zipper-interacting protein kinase (ZIPK) and integrin-linked kinase (ILK) at 54-59 kDa in the cytoskeleton and membrane fractions. Cytoskeletal ZIPK and ILK were separated and partially purified by chromatography on SP-Sepharose and on MonoQ. ZIPK preferentially phosphorylated MLC20 and had low activity on MYPT1. ILK phosphorylated both MLC20 and MYPT1 and phosphorylation of MYPT1 occured on Thr-695. The above results raise the potential for regulation of MP activity in platelet cytoskeleton by ILK and suggest an alternative to the Rho-linked pathway.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Biochemical Journal. - 365 : 1 (2002), p. 79-87. -
További szerzők:Murányi Andrea (1966-) (biokémikus) Ito, Masaaki Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus) Csortos Csilla (1956-) (biokémikus) Gergely Pál (1947-) (biokémikus)
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4.

001-es BibID:BIBFORM028725
Első szerző:Murányi Andrea (biokémikus)
Cím:Phosphorylation of the myosin phosphatase target subunit by integrin-linked kinase / Andrea Murányi, Justin A. MacDonald, Jing Ti Deng, David P. Wilson, Timothy A. J. Haystead, Michael P. Walsh, Ferenc Erdődi, Enikő Kiss, Yue Wu, David J. Hartshorne
Dátum:2002
ISSN:0264-6021
Megjegyzések:A mechanism proposed for regulation of myosin phosphatase (MP) activity is phosphorylation of the myosin phosphatase target subunit (MYPT1). Integrin-linked kinase (ILK) is associated with the contractile machinery and can phosphorylate myosin at the myosin light-chain kinase sites. The possibility that ILK may also phosphorylate and regulate MP was investigated. ILK was associated with the MP holoenzyme, shown by Western blots and in-gel kinase assays. MYPT1 was phosphorylated by ILK and phosphorylation sites in the N- and C-terminal fragments of MYPT1 were detected. From sequence analyses, three sites were identified: a primary site at Thr(709), and two other sites at Thr(695) and Thr(495). One of the sites for cAMP-dependent protein kinase (PKA) was Ser(694). Assays with the catalytic subunit of type 1 phosphatase indicated that only the C-terminal fragment of MYPT1 phosphorylated by zipper-interacting protein kinase, and ILK inhibited activity. The phosphorylated N-terminal fragment activated phosphatase activity and phosphorylation by PKA was without effect. Using full-length MYPT1 constructs phosphorylated by various kinases it was shown that Rho kinase gave marked inhibition; ILK produced an intermediate level of inhibition, which was considerably reduced for the Thr(695)-->Ala mutant; and PKA had no effect. In summary, phosphorylation of the various sites indicated that Thr(695) was the major inhibitory site, Thr(709) had only a slight inhibitory effect and Ser(694) had no effect. The findings that ILK phosphorylated both MYPT1 and myosin and the association of ILK with MP suggest that ILK may influence cytoskeletal structure or function.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
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Megjelenés:Biochemical Journal. - 366 (2002), p. 211-216. -
További szerzők:MacDonald, Justin A. Deng, Jing Ti Wilson, David P. Haystead, Timothy A. J. Walsh, Michael P. Kiss Enikő Wu, Yue Hartshorne, David J. Erdődi Ferenc (1953-) (biokémikus)
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5.

001-es BibID:BIBFORM028850
Első szerző:Tóth Attila (biológus)
Cím:Phosphorylation of MYPT1 by protein kinase C attenuates interaction with PP1 catalytic subunit and the 20 kDa light chain of myosin / Attila Tóth, Enikő Kiss, Pál Gergely, Michael P. Walsh, David J. Hartshorne, Ferenc Erdődi
Dátum:2000
ISSN:0014-5793
Megjegyzések:Abstract The effect of phosphorylation in the N-terminal region of myosin phosphatase target subunit 1 (MYPT1) on the interactions with protein phosphatase 1 catalytic subunit (PP1c) and with phosphorylated 20 kDa myosin light chain (P-MLC20) was studied. Protein kinase C (PKC) phosphorylated threonine-34 (1 mol/mol), the residue preceding the consensus PP1c-binding motif ((35)KVKF(38)) in MYPT1(1-38), but this did not affect binding of the peptide to PP1c. PKC incorporated 2 mol P(i) into MYPT1(1-296) suggesting a second site of phosphorylation within the ankyrin repeats (residues 40-296). This phosphorylation diminished the stimulatory effect of MYPT1(1-296) on the P-MLC20 phosphatase activity of PP1c. Binding of PP1c or P-MLC20 to phosphorylated MYPT1(1-296) was also attenuated. It is concluded that phosphorylation of MYPT1 by PKC may therefore result in altered dephosphorylation of myosin.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Febs Letters. - 484 : 2 (2000), p. 113-117. -
További szerzők:Kiss Enikő Walsh, Michael P. Hartshorne, David J. Gergely Pál (1947-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus)
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6.

001-es BibID:BIBFORM028849
Első szerző:Tóth Attila (biológus)
Cím:Study of the subunit interactions in myosin phosphatase by surface plasmon resonance / Attila Tóth, Enikő Kiss, Friedrich W. Herberg, Pál Gergely, David J. Hartshorne, Ferenc Erdődi
Dátum:2000
ISSN:1432-1033
Megjegyzések:he interactions of the catalytic subunit of type 1 protein phosphatase (PP1c) and the N-terminal half (residues 1-511) of myosin phosphatase target subunit 1 (MYPT1) were studied. Biotinylated MYPT1 derivatives were immobilized on streptavidin-biosensor chips, and binding parameters with PP1c were determined by surface plasmon resonance (SPR). The affinity of binding of PP1c was: MYPT11-296 > MYPT11-38 > MYPT123-38. No binding was detected with MYPT11-34, suggesting a critical role for residues 35-38, i.e. the PP1c binding motif. Binding of residues 1-22 was inferred from: a higher affinity binding to PP1c for MYPT11-38 compared to MYPT123-38, as deduced from SPR kinetic data and ligand competition assays; and an activation of the myosin light chain phosphatase activity of PP1c by MYPT11-38, but not by MYPT123-38. Residues 40-296 (ankyrin repeats) in MYPT11-296 inhibited the phosphorylase phosphatase activity of PP1c (IC50 = 0.2 nM), whereas MYPT11-38, MYPT123-38 or MYPT11-34 were without effect. MYPT140-511, which alone did not bind to PP1c, showed facilitated binding to the complexes of PP1c-MYPT11-38 and PP1c-MYPT123-38. The inhibitory effect of MYPT140-511 on the phosphorylase phosphatase activity of PP1c also was increased in the presence of MYPT11-38. The binding of MYPT1304-511 to complexes of PP1c and MYPT11-38, or MYPT11-296, was detected by SPR. These results suggest that within the N-terminal half of MYPT1 there are at least four binding sites for PP1c. The essential interaction is with the PP1c-binding motif and the other interactions are facilitated in an ordered and cooperative manner.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:European Journal Of Biochemistry. - 267 : 6 (2000), p. 1687-1697. -
További szerzők:Kiss Enikő Herberg, Friedrich W. Hartshorne, David J. Gergely Pál (1947-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus)
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