The regulatory subunit of protein kinase CK2 is a specific A‐Raf activator

Hagemann, Carsten; Kalmes, Andreas; Wixler, Viktor; Wixler, Ludmilla; Schuster, Tillman; Rapp, Ulf R.

doi:10.1016/s0014-5793(97)00011-2

Cited by 81 publications

(64 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Similar conclusions have been reached using thermosensitive mutants of the CK2a subunit in yeast [12]. Very recently, yeast two-hybrid analysis has been used to demonstrate the interaction of CK2P with A-Raf [13,14] and with mos [15]. Both A-Raf and mos are cytoplasmic oncogene products that have Ser/Thr protein kinase activity that phosphorylate and activate MEK and are therefore involved in the transduction of the stimuli that trigger cell division.…”

Section: Introductionsupporting

confidence: 53%

An inactive mutant of the α subunit of protein kinase CK2 that traps the regulatory CK2β subunit

et al. 1997

View full text Add to dashboard Cite

show abstract

Section: Introductionsupporting

confidence: 53%

An inactive mutant of the α subunit of protein kinase CK2 that traps the regulatory CK2β subunit

et al. 1997

View full text Add to dashboard Cite

show abstract

“…It is possible that the C-terminus of CK2b recognizes a common structural motif of serine/threonine kinases. However, the fact that CK2b interacts specifically with A-Raf (Boldyreff and Issinger, 1997) but not c-Raf (Chen et al, 1997;Hagemann et al, 1997), suggests that kinase interaction with CK2b may require higher specificity. The structure determination of the human Chk1 kinase (Chen et al, 2000) has indicated that the activity of the kinase domain (residues 1-265) of human Chk1 is over 20-fold more active than the full-length Chk1 kinase toward Cdc25C substrate.…”

Section: Discussionmentioning

confidence: 99%

Modulation of human checkpoint kinase Chk1 by the regulatory β-subunit of protein kinase CK2

2003

View full text Add to dashboard Cite

Protein kinase CK2 is a serine/threonine protein kinase involved in various aspects of cellular regulation. The regulatory b-subunit of CK2 exerts a central role not only in mediating formation of tetrameric CK2 complexes but also as a docking partner for several protein kinases. In this study, CK2b is found to interact with the human cell cycle checkpoint kinase Chk1. The Chk1-interacting region of CK2b is localized at the C-terminus and the complex between CK2b and Chk1 is devoid of the catalytic CK2a-subunit. The interaction between CK2b and Chk1 leads to an increase in the Cdc25C phosphorylation activity of Chk1. The screening of several cell lines has revealed that the association between CK2b and Chk1 also occurs in vivo at a different degree. Collectively, these studies confirm the implication of the regulatory b-subunit of protein kinase CK2 in cell cycle regulation and identify a novel mechanism for the activation of Chk1 protein kinase.

show abstract

“…Yeast Two-hybrid Screening-Full-length Btk was cloned into pPCH1 (19) and used as a bait. HF7c yeast cells expressing the bait vector were transformed (20) with a human splenic library.…”

Section: Methodsmentioning

confidence: 99%

Bruton's Tyrosine Kinase Is a Toll/Interleukin-1 Receptor Domain-binding Protein That Participates in Nuclear Factor κB Activation by Toll-like Receptor 4

Jefferies

Doyle

Brunner

et al. 2003

Journal of Biological Chemistry

267

249

View full text Add to dashboard Cite

The Tec family of protein tyrosine kinases, of which Bruton's tyrosine kinase (Btk) 1 is a prototypical member, is involved in a vast array of signaling pathways in cells of hematopoietic lineage. Btk is expressed in all hematopoietic cells except T lymphocytes and natural killer cells. It is critically important for B-cell development as well as mature B-cell activation and survival. It has also been shown to be important for IgEmediated activation of mast cells resulting in allergic reactions. Btk kinase activity and tyrosine phosphorylation have both been shown to increase upon cross-linking or stimulation of the B-cell receptor, the IgE receptor (Fc⑀RII), and a number of cytokine receptors such as those for IL-3, IL-5, IL-6, and IL-10, suggesting a general role for Btk in immune regulation (1-4). Whereas the molecular mechanisms by which the B-cell receptor regulates B-cell proliferation and survival are not well understood, Btk has recently been shown to lie downstream of the B-cell receptor on the pathway regulating activation of the key pro-inflammatory transcription factor NF B (5-8). The biological importance of the signaling function has been shown by naturally occurring loss of function mutations in Btk in human X-linked agammaglobulinemia and its murine counterpart, X-linked immunodeficiency (Xid). These diseases are characterized by a block in B-cell development and defects in B-cell signaling, and in X-linked agammaglobulinemia patients, mutations in Btk are associated associated with an increased frequency of bacterial infections in all organs (9). Studies in Xid mice have also shown reduced responses to LPS stimulation, with nitric oxide (NO) production decreased, and macrophage effector functions impaired (10 -12). This, coupled with the observation that responses to T-independent antigens are impaired in Xid mice, suggests a role for Btk in innate immune responses.Toll-like receptors (TLRs) have an essential function in both innate and adaptive immunity and have evolved to recognize, with high specificity, diverse microbial pathogens (13). TLR4, as the receptor for the Gram-negative bacterial product LPS, is the prototypical member of the family (numbered TLR1-10 in humans) of type I transmembrane receptors, which are characterized by an extracellular leucine-rich repeat domain and an intracellular Toll/IL-1 receptor (TIR) domain, responsible for signaling. Ligands for other family members (except TLR10) have been identified and include bacterial flagellin and unmethylated bacterial CpG motifs for TLR5 and TLR9, respectively; double-stranded RNA for TLR3; and the antiviral compound R-848 recognizing TLR7 and TLR8. Research into how these receptors signal has identified MyD88 and IL-1-receptorassociated kinases (IRAKs) as key proximal signaling components regulating activation of the pro-inflammatory transcription factor NF B in response to LPS (reviewed in Ref. 14). Important differences in the proteins recruited to the different TLR members have also been described. Both TLR2 (the receptor for...

show abstract

The regulatory subunit of protein kinase CK2 is a specific A‐Raf activator

Cited by 81 publications

References 22 publications

An inactive mutant of the α subunit of protein kinase CK2 that traps the regulatory CK2β subunit

An inactive mutant of the α subunit of protein kinase CK2 that traps the regulatory CK2β subunit

Modulation of human checkpoint kinase Chk1 by the regulatory β-subunit of protein kinase CK2

Bruton's Tyrosine Kinase Is a Toll/Interleukin-1 Receptor Domain-binding Protein That Participates in Nuclear Factor κB Activation by Toll-like Receptor 4

Contact Info

Product

Resources

About