[42] Criteria for the classification of protein kinases

Traugh, Jolinda A.; Ashby, C. Dennis; Walsx, D.A.

doi:10.1016/0076-6879(74)38045-7

Cited by 43 publications

(18 citation statements)

References 15 publications

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“…The projection-associated activity had the properties of a cAMP-dependent holoenzyme (42). It was dramatically stimulated by cAMP and was almost completely blocked by the inhibitor protein of Walsh et al (46).…”

Section: Molecular Properties Of the Camp-dependent Map 2 Kinasementioning

confidence: 90%

A protein kinase bound to the projection portion of MAP 2 (microtubule-associated protein 2)

Vallee¹,

DiBartolomeis²,

Theurkauf³

1981

The Journal of Cell Biology

239

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In previous work we have demonstrated that the microtubule-associated protein 2 (MAP 2) molecule consists of two structural parts. One part of the molecule, referred to as the assembly-promoting domain, binds to the microtubule surface and is responsible for promoting microtubule assembly ; the other represents a filamentous projection observed on the microtubule surface that may be involved in the interaction of microtubules with other cellular structures . MAP 2 is known to be specifically phosphorylated as the result of a protein kinase activity that is present in microtubule preparations . We have now found that the activity copurifies with the projection portion of MAP 2 itself . Kinase activity coeluted with MAP 2 when microtubule protein was subjected to either gel-filtration chromatography on Bio-Gel A15m or ion-exchange chromatography on DEAE-Sephadex. The activity was released from microtubules by mild digestion with chymotrypsin in parallel with the removal by the protease of the MAP 2 projections from the microtubule surface . The association of the activity with the projection was demonstrated directly by gel filtration chromatography of the projections on Bio-Gel A-15m . Three protein species (Mr = 39,000, 55,000, and 70,000) cofractionated with MAP 2, and two of these (Mr = 39,000 and 55,000) may represent the subunits of an associated cyclic AMP-dependent protein kinase . The projection-associated activity was stimulated 10-fold by cyclic AMP and was inhibited >95% by the cyclic AMP-dependent protein kinase inhibitor from rabbit skeletal muscle . It appeared to represent the only significant activity associated with microtubules, almost no activity being found with tubulin, other MAPS, or the assembly-promoting domain of MAP 2, and was estimated to account for 7-22% of the total brain cytosolic protein kinase activity . The location of the kinase on the projection is consistent with a role in regulating the function of the projection, though other roles for the enzyme are also possible .

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Section: Molecular Properties Of the Camp-dependent Map 2 Kinasementioning

confidence: 90%

A protein kinase bound to the projection portion of MAP 2 (microtubule-associated protein 2)

Vallee¹,

DiBartolomeis²,

Theurkauf³

1981

The Journal of Cell Biology

239

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“…Previous attempts to detect cyclic AMP-dependent protein kinase in rat liver nuclei [21,22,42,50,51] or rat mammary gland nuclei [23] may have been unsuccessful due to the relatively large quantity of nuclear cyclic-AMP-independent protein kinase activity obscuring small amounts of the cyclic-AMPdependent enzyme; by the observed instability of isolated nuclear cyclic-AMP-dependent protein kinase (A. M. Spielvogel and R. A. Jungmann, unpublished observation); and by the lack of documentation of the presence of dissociated catalytic subunits according to all of the criteria given by Traugh et al [55]. It is also conceivable that appreciable quantities of cyclic-AMP-dependent protein kinase (or the dissociated catalytic subunit) can be detected only at certain times during hormonal stimulation of RNA synthesis and after the cyclic-AMP-mediated translocation and compartmentalization of cytoplasmic cyclic-AMP-dependent protein kinase at nuclear sites.…”

Section: Discussionmentioning

confidence: 99%

“…Traugh et al [55] have established the following four criteria for the classification of protein kinase : (a) stimulation by cyclic AMP; (b) binding of cyclic AMP; (c) inhibition of the catalytic activity by the regulatory subunit; and (d) inhibition of the catalytic activity by the heatstable protein kinase inhibitor from skeletal muscle. On the basis of three of these criteria the nuclear ovarian protein kinase I1 may be classified as cyclic-AMP-dependent protein kinase.…”

Section: Discussionmentioning

confidence: 99%

Evidence for the Identity of Nuclear and Cytoplasmic Adenosine-3':5'-Monophosphate-Dependent Protein Kinase from Porcine Ovaries and Nuclear Translocation of the Cytoplasmic Enzyme

et al. 1977

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Protein phosphokinase activity from a 0.5 M NaCl extract of purified porcine ovary nuclei has been resolved by Sephadex G-200 gel filtration into three forms of protein kinase, protein kinase I and 111, both independent of adenosine 3' : 5'-monophosphate (cyclic AMP), and cyclic-AMPdependent protein kinase 11. Cyclic AMP-binding activity was associated with protein kinase I1 but not with protein kinases I and 111. Protein kinases I, 11, and I11 exhibited different cyclic nucleotide dependency and substrate specificity. Protein kinase I1 was inhibited by a*heat-stable protein from rabbit skeletal muscle, whereas protein kinases I and I11 were not inhibited. Evidence for the identity of nuclear cyclic-AMP-dependent protein kinase I1 with cytosol (105 000 x g supernatant fraction) cyclic-AMP-dependent protein kinase was obtained in several ways. Nuclear and cytosol cyclic-AMP-dependent protein kinases exhibited identical elution characteristics on DEAE-cellulose and Sephadex G-200 indicating that both kinases are of similar molecular size and possess similar ionic charge. Both kinases exhibited an identical K , for ATP of 8 pM, showed similar substrate specificity, and revealed similar antigenic properties. Cyclic-AMP-dependent protein kinase I1 was also identified in nuclei isolated in nonaqueous media, eliminating the possibility that the cyclic-AMP-dependent protein kinase activity identified in nuclei isolated in aqueous media may have arisen as the result of cytoplasmic contamination.After incubation of neonatal porcine ovaries which lack nuclear cyclic-AMP-dependent protein kinase with 0.1 pM 8-p-chlorophenylthio cyclic AMP, considerable cyclic-AMP-dependent protein kinase I1 activity was identified in nuclei isolated in nonaqueous media. From these data it is concluded that the nuclear cyclic-AMP-dependent protein kinase I1 is related to or identical with the ovary cytoplasmic cyclic-AMP-dependent protein kinase, supporting the concept that nuclear cyclic-AMPdependent protein kinase is of cytoplasmic origin.

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“…While the intracellular cAMP concentration stays at a low level, the association of the PKA heterotetramer subunits is maintainable by the binding between the catalytic domain of the catalytic subunits and the pseudo-substrate sequence of the regulatory subunits. At elevation of the intracellular cAMP level owing to either activation of adenylyl cyclases or inactivation of phosphodiesterases, however, the PKA dissociates, yielding the active form of the catalytic subunits [16]. The catalytic subunits of PKA are partially active at this step and subsequently become fully active by autophosphorylation at the Thr-197 residue of the activation loop.…”

mentioning

confidence: 99%

Calyculin A-Sensitive Protein Phosphatases are Involved in Maintenance of Progressive Movement in Mouse Spermatozoa In Vitro by Suppression of Autophosphorylation of Protein Kinase A

Goto

Harayama

2009

J. Reprod. Dev.

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Abstract. Protein serine/threonine phosphorylation in mammalian sperm flagella has been considered to play important roles in regulation of motility. Protein phosphorylation state reflects balance of enzymatic activities between protein phosphatases and protein kinases [predominantly protein kinase A (PKA)]. The aims of this study were to disclose roles of protein phosphatases in the regulation of sperm motility and to provide evidence for suppression of PKA full activation by protein phosphatases in sperm flagella. Mouse epididymal spermatozoa were incubated with a cell-permeable protein phosphatase 1 (PP1)/protein phosphatase 2A (PP2A) inhibitor (calyculin A: 25-125 nM) at 37.5 C. After incubation, they were used for immunodetection of phosphorylated proteins, PKA and PP1γ2, assessment for motility and co-immunoprecipitation of PP1γ2 with PKA. Incubation with calyculin A enhanced the phosphorylation states of several proteins (>250 kDa, 170 kDa, 155 kDa, 140 kDa and 42 kDa for serine/threonine phosphorylation and 70 kDa for tyrosine phosphorylation) and PKA catalytic subunits [at the autophosphorylation residue (Thr-197) for its full enzymatic activation] in the flagella. Coincidently, this incubation induced changes of sperm flagellar movement from the progressive type to the hyperactivation-like type. Indirect immunofluorescence and co-immunoprecipitation showed that PKA was co-localized with PP1γ2 in the principal pieces of sperm flagella. These findings suggest that calyculin A-sensitive protein phosphatases (PP1/PP2A) suppress full activation of PKA as well as enhancement of the phosphorylation states of other flagellar proteins in sperm flagella in order to prevent precocious changes of flagellar movement from the progressive type to hyperactivation. Key words: Cyclic adenosine 3',5'-monophosphate (cAMP), Hyperactivation, Protein kinase, Protein phosphatase 1 (PP1), Protein phosphorylation (J. Reprod. Dev. 55: [327][328][329][330][331][332][333][334] 2009) ammalian spermatozoa are differentiated from spermatogonia in the testicular seminiferous tubules and then transferred through the duct of the epididymis. By arrival in the caudal epididymides, they have acquired the potentials to move in a forward direction, bind with the zona pellucida and fertilize oocytes [1], but they are temporally quieted in the epididymis by the influence of the acidic-base status of the luminal fluid [2,3] and interaction with membrane stabilizing factors [4,5]. After ejaculation into the female reproductive tract, the spermatozoa quickly initiate flagellar beating, which is regulated by the protein serine [Ser (S)]/threonine [Thr (T)] phosphorylation in the flagella [6]. Some of the phosphorylated proteins have previously been identified as dynein [6,7] and axokinin [8]. Subsequently, they gradually undergo a series of changes in their intracellular spaces as well as on their cell surfaces (capacitation), including dissociation of decapacitation factors (e.g., cholesterol and acrosomal stabilizing factors), elevation of th...

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[42] Criteria for the classification of protein kinases

Cited by 43 publications

References 15 publications

A protein kinase bound to the projection portion of MAP 2 (microtubule-associated protein 2)

A protein kinase bound to the projection portion of MAP 2 (microtubule-associated protein 2)

Evidence for the Identity of Nuclear and Cytoplasmic Adenosine-3':5'-Monophosphate-Dependent Protein Kinase from Porcine Ovaries and Nuclear Translocation of the Cytoplasmic Enzyme

Calyculin A-Sensitive Protein Phosphatases are Involved in Maintenance of Progressive Movement in Mouse Spermatozoa In Vitro by Suppression of Autophosphorylation of Protein Kinase A

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