Myosin phosphatase interacts with and dephosphorylates the retinoblastoma protein in THP-1 leukemic cells: Its inhibition is involved in the attenuation of daunorubicin-induced cell death by calyculin-A

Kiss, Andrea; Lontay, Beáta; Bécsi, Bálint; Márkász, László; Oláh, Éva; Gergely, Pál; Erdõdi, Ferenc

doi:10.1016/j.cellsig.2008.07.018

Cited by 36 publications

(29 citation statements)

References 47 publications

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“…In principle, Phactr1 could act directly, as an MLCP inhibitor. Given the cytoplasmic location of MLCP it is perhaps more likely that it acts indirectly, although MYPT-PP1 complexes have been reported to mediate nuclear events (Kiss et al, 2008;Bollen et al, 2010). For example, nuclear Phactr1 might act positively as part of a PP1 holoenzyme regulating pathways indirectly controlling levels of phosphorylated MLC (Fig.…”

Section: Discussionmentioning

confidence: 99%

G-actin regulates the shuttling and PP1 binding of the RPEL protein Phactr1 to control actomyosin assembly

Wiezlak

Diring²,

Abella

et al. 2012

Journal of Cell Science

111

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SummaryThe Phactr family of PP1-binding proteins is implicated in human diseases including Parkinson's, cancer and myocardial infarction. Each Phactr protein contains four G-actin binding RPEL motifs, including an N-terminal motif, abutting a basic element, and a Cterminal triple RPEL repeat, which overlaps a conserved C-terminus required for interaction with PP1. RPEL motifs are also found in the regulatory domains of the MRTF transcriptional coactivators, where they control MRTF subcellular localisation and activity by sensing signal-induced changes in G-actin concentration. However, whether G-actin binding controls Phactr protein function -and its relation to signalling -has not been investigated. Here, we show that Rho-actin signalling induced by serum stimulation promotes the nuclear accumulation of Phactr1, but not other Phactr family members. Actin binding by the three Phactr1 C-terminal RPEL motifs is required for Phactr1 cytoplasmic localisation in resting cells. Phactr1 nuclear accumulation is importin a-b dependent. G-actin and importin a-b bind competitively to nuclear import signals associated with the N-and C-terminal RPEL motifs. All four motifs are required for the inhibition of serum-induced Phactr1 nuclear accumulation when G-actin is elevated. G-actin and PP1 bind competitively to the Phactr1 C-terminal region, and Phactr1 C-terminal RPEL mutants that cannot bind G-actin induce aberrant actomyosin structures dependent on their nuclear accumulation and on PP1 binding. In CHL-1 melanoma cells, Phactr1 exhibits actin-regulated subcellular localisation and is required for stress fibre assembly, motility and invasiveness. These data support a role for Phactr1 in actomyosin assembly and suggest that Phactr1 G-actin sensing allows its coordination with F-actin availability.

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Section: Discussionmentioning

confidence: 99%

G-actin regulates the shuttling and PP1 binding of the RPEL protein Phactr1 to control actomyosin assembly

Wiezlak

Diring²,

Abella

et al. 2012

Journal of Cell Science

111

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“…PP2A inhibition influenced caspase-3 activation [13]. Therefore, we ex- illustrates that CLA and TM elevated caspase-3 activity significantly; 389 however, the extent of activation was substantially higher in case of 390 CLA (4.5-fold) compared to TM (1.5-fold).…”

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confidence: 99%

“…PP1c binds tightly to the C-terminal re-617 gion of pRb to a PP1c-binding motif-like sequence and forms an active 618 complex functional with respect to dephosphorylation of phosphorylat-619 ed residues in pRb [21]. However, a competition between PP1c regulato-620 ry subunits and pRb for PP1c-binding is assumed [13] Fig. 4D), but not MYPT1 (see Fig.…”

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confidence: 99%

“…In our previous study, we showed that the C-terminal phosphoryla- PP1 holoenzyme acting on phospho-pRb in THP-1 leukemic cells [13].…”

mentioning

confidence: 99%

“…Accumulating lines of evidence suggest that PP1 is the major pRb 614 phosphatase in cells [10, [22][23][24], however, the mechanisms via PP1 de-615 phosphorylates pRb are still not clearly established and alternative 616 routes might exist [13,21,43]. PP1c binds tightly to the C-terminal re-617 gion of pRb to a PP1c-binding motif-like sequence and forms an active 618 complex functional with respect to dephosphorylation of phosphorylat-619 ed residues in pRb [21].…”

mentioning

confidence: 99%

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Inhibition of protein phosphatase-1 and -2A decreases the chemosensitivity of leukemic cells to chemotherapeutic drugs

Dedinszki

Kiss

Márkász

et al. 2015

Cellular Signalling

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Grading the commercial optical biosensor literature—Class of 2008: ‘The Mighty Binders’

Rich

Myszka

2009

J of Molecular Recognition

141

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Optical biosensor technology continues to be the method of choice for label-free, real-time interaction analysis. But when it comes to improving the quality of the biosensor literature, education should be fundamental. Of the 1413 articles published in 2008, less than 30% would pass the requirements for high-school chemistry. To teach by example, we spotlight 10 papers that illustrate how to implement the technology properly. Then we grade every paper published in 2008 on a scale from A to F and outline what features make a biosensor article fabulous, middling or abysmal. To help improve the quality of published data, we focus on a few experimental, analysis and presentation mistakes that are alarmingly common. With the literature as a guide, we want to ensure that no user is left behind.

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Myosin phosphatase interacts with and dephosphorylates the retinoblastoma protein in THP-1 leukemic cells: Its inhibition is involved in the attenuation of daunorubicin-induced cell death by calyculin-A

Cited by 36 publications

References 47 publications

G-actin regulates the shuttling and PP1 binding of the RPEL protein Phactr1 to control actomyosin assembly

G-actin regulates the shuttling and PP1 binding of the RPEL protein Phactr1 to control actomyosin assembly

Inhibition of protein phosphatase-1 and -2A decreases the chemosensitivity of leukemic cells to chemotherapeutic drugs

Grading the commercial optical biosensor literature—Class of 2008: ‘The Mighty Binders’

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