Two different protein kinases act on a different time schedule as glial filament kinases during mitosis.

Matsuoka, Yoichiro; Nishizawa, Kunihide; Yano, Takeo; Shibata, Masao; Ando, Shoji; Takahashi, Toshitada; Inagaki, Masaki

doi:10.1002/j.1460-2075.1992.tb05358.x

Cited by 96 publications

(77 citation statements)

References 46 publications

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“…Immunocytochemical studies using TM38 and TM71 revealed that these two sites were phosphorylated at the cleavage furrow during cytokinesis in U251 human glioma cells (Figure 1c and d). Together with previous immunocytochemical studies (Matsuoka et al, 1992;Tsujimura et al, 1994;Ogawara et al, 1995;Takai et al, 1996;Sekimata et al, 1996;Inagaki et al, 1997b) (Table 1).…”

supporting

confidence: 80%

“…Using site-and phosphorylation state-speci®c antibodies (Inagaki et al, 1997a), we previously detected cleavage furrow kinase (CF kinase) activity that phosphorylates Thr 7 , Ser 13 and Ser 38 on human glial ®brillary acidic protein (GFAP) at the cleavage furrow during cytokinesis (Matsuoka et al, 1992). This protein kinase activity was observed not only in astroglial cells but also in other cultured cells in which GFAP was ectopically expressed (Sekimata et al, 1996).…”

mentioning

confidence: 99%

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Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: cleavage furrow-specific phosphorylation of intermediate filaments

et al. 1999

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The small GTPase Rho and one of its targets, Rhoassociated kinase (Rho-kinase), are implicated in a wide spectrum of cellular functions, including cytoskeletal rearrangements, transcriptional activation and smooth muscle contraction. Since Rho also plays an essential role in cytokinesis, Rho-kinase may possibly mediate some biological aspects of cytokinesis. Here, using a series of monoclonal antibodies that can speci®cally recognize distinct phosphorylated sites on glial ®brillary acidic protein (GFAP) and vimentin, phosphorylation sites by Rho-kinase in vitro were revealed to be identical to in vivo phosphorylation sites on these intermediate ®lament (IF) proteins at the cleavage furrow in dividing cells. We then found, by preparing two types of antiRho-kinase antibodies, that Rho-kinase accumulated highly and circumferentially at the cleavage furrow in various cell lines. This subcellular distribution during cytokinesis was very similar to that of ezrin/radixin/ moesin (ERM) proteins and Ser 19 -phosphorylated myosin light chain. These results raise the possibility that Rhokinase might be involved in the formation of the contractile ring by modulating these F-actin-binding proteins during cytokinesis and in the phosphorylation and regulation of IF proteins at the cleavage furrow.

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supporting

confidence: 80%

mentioning

confidence: 99%

Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: cleavage furrow-specific phosphorylation of intermediate filaments

et al. 1999

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“…Three sites that are phosphorylated late in the M phase were detected on glial fibrillary acidic protein, a component of intermediate filaments. These sites are phosphorylated in vitro by PKA but not by protein kinase C (26). Thus the glial fibrillary acidic protein may be phosphorylated by the same mitotic kinase that phosphorylates the POU proteins.…”

Section: Discussionmentioning

confidence: 98%

M-Phase-Specific Phosphorylation of the POU Transcription Factor GHF-1 by a Cell Cycle-Regulated Protein Kinase Inhibits DNA Binding

Caelles

Hennemann

Karin

1995

Molecular and Cellular Biology

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GHF-1 is a member of the POU family of homeodomain proteins. It is a cell-type-specific transcription factor responsible for determination and expansion of growth hormone (GH)-and prolactin-expressing cells in the anterior pituitary. It was previously suggested that cyclic AMP (cAMP)-responsive protein kinase A (PKA) phosphorylates GHF-1 at a site within the N-terminal arm of its homeodomain, thereby inhibiting its binding to the GH promoter. These results, however, are inconsistent with the physiological stimulation of GH production by the cAMP pathway. As reported here, cAMP agonists and PKA do not inhibit GHF-1 activity in living cells and although they stimulate the phosphorylation of GHF-1, the inhibitory phosphoacceptor site within the homeodomain is not affected. Instead, this site, Thr-220, is subject to M-phase-specific phosphorylation. As a result, GHF-1 DNA binding activity is transiently inhibited during the M phase. This activity is regained once cells enter G 1 , a phase during which GHF-1 phosphorylation is minimal. Thr-220 of GHF-1 is the homolog of the mitotic phosphoacceptor site responsible for the M-phase-specific inhibition of Oct-1 DNA binding Ser-382. As this site is conserved in all POU proteins, it appears that all members of this group are similarly regulated. A specific kinase activity distinct in its substrate specificity and susceptibility to inhibitors from the Cdc2 mitotic kinase or PKA was identified in extracts of mitotic cells. This novel activity could be involved in regulating the DNA binding activity of all POU proteins in a cell cycle-dependent manner.

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“…Previous studies have created pGFAP antibodies, some of which are commercially available [40,41]. In this study, we generated and characterised our polyclonal antibodies against p8GFAP and p13GFAP to ensure that they detected only the phosphorylated form of GFAP, and that this phosphoprotein was detectable in astrocytes in the pig brain.…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of GFAP is Associated with Injury in the Neonatal Pig Hypoxic-Ischemic Brain

Sullivan

Miller

et al. 2012

Neurochem Res

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Glial fibrillary acidic protein (GFAP) is an intermediate filament protein expressed in the astrocytecytoskeleton that plays an important role in the structure and function of the cell. GFAP can be phosphorylated at six serine (Ser) or threonine (Thr) residues but little is known about the role of GFAP phosphorylation in physiological and pathophysiological states. We have generated antibodies against two phosphorylated GFAP (pGFAP) proteins: p8GFAP, where GFAP is phosphorylated at Ser-8 and p13GFAP, where GFAP is phosphorylated at Ser-13. We examined p8GFAP and p13GFAP expression in the control neonatal pig brain and at 24h and 72h after an hypoxic-ischemic (HI) insult. Immunohistochemistry demonstrated pGFAP expression in astrocytes with an atypical cytoskeletal morphology, even in control brains. Semi-quantitative western blotting revealed that p8GFAP expression was significantly increased at 24h post-insult in HI animals with seizures in frontal, parietal, temporal and occipital cortices. At 72h post-insult, p8GFAP and p13GFAP expression were significantly increased in HI animals with seizures in brain regions that are vulnerable to cellular damage (cortex and basal ganglia), but no changes were observed in brain regions that are relatively spared following an HI insult (brain stem and cerebellum). Increased pGFAP expression was associated with poor neurological outcomes such as abnormal encephalography (EEG) and neurobehaviour, and increased histological brain damage.Phosphorylation of GFAP may play an important role in astrocyte remodelling during development and disease and could potentially contribute to the plasticity of the central nervous system. 3

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Two different protein kinases act on a different time schedule as glial filament kinases during mitosis.

Cited by 96 publications

References 46 publications

Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: cleavage furrow-specific phosphorylation of intermediate filaments

Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: cleavage furrow-specific phosphorylation of intermediate filaments

M-Phase-Specific Phosphorylation of the POU Transcription Factor GHF-1 by a Cell Cycle-Regulated Protein Kinase Inhibits DNA Binding

Phosphorylation of GFAP is Associated with Injury in the Neonatal Pig Hypoxic-Ischemic Brain

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