Nikolai Malinin
Weizmann Institute of Science
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Featured researches published by Nikolai Malinin.
Molecular and Cellular Biology | 1999
Helmut Holtmann; Reinhard Winzen; Pamela M. Holland; Solveig Eickemeier; Elke Hoffmann; David Wallach; Nikolai Malinin; Jonathan A. Cooper; Klaus Resch; Michael Kracht
ABSTRACT A hallmark of inflammation is the burst-like formation of certain proteins, initiated by cellular stress and proinflammatory cytokines like interleukin 1 (IL-1) and tumor necrosis factor, stimuli which simultaneously activate different mitogen-activated protein (MAP) kinases and NF-κB. Cooperation of these signaling pathways to induce formation of IL-8, a prototype chemokine which causes leukocyte migration and activation, was investigated by expressing active and inactive forms of protein kinases. Constitutively active MAP kinase kinase 7 (MKK7), an activator of the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) pathway, induced IL-8 synthesis and transcription from a minimal IL-8 promoter. Furthermore, MKK7 synergized in both effects with NF-κB-inducing kinase (NIK). Activation of the IL-8 promoter by either of the kinases required functional NF-κB and AP-1 sites. While NIK and MKK7 did not affect degradation of IL-8 mRNA, an active form of MKK6, which selectively activates p38 MAP kinase, induced marked stabilization of the transcript and further increased IL-8 protein formation induced by NIK plus MKK7. Consistently, the MAP kinase kinase kinase MEKK1, which can activate NF-κB, SAPK/JNK, and p38 MAP kinases, most potently induced IL-8 formation. These results provide evidence that maximal IL-8 gene expression requires the coordinate action of at least three different signal transduction pathways which cooperate to induce mRNA synthesis and suppress mRNA degradation.
Journal of Biological Chemistry | 1998
Hisaya Akiba; Hiroyasu Nakano; Shigeyuki Nishinaka; Masahisa Shindo; Tetsuji Kobata; Machiko Atsuta; Chikao Morimoto; Carl F. Ware; Nikolai Malinin; David Wallach; Hideo Yagita; Ko Okumura
CD27 is a member of the tumor necrosis factor (TNF) receptor superfamily and is expressed on T, B, and NK cells. The signal via CD27 plays pivotal roles in T-T and T-B cell interactions. Here we demonstrate that overexpression of CD27 activates NF-κB and stress-activated protein kinase (SAPK)/c-Jun N-terminal kinase (JNK). Deletion analysis of the cytoplasmic domain of CD27 revealed that the C-terminal PIQEDYR motif was indispensable for both NF-κB and SAPK/JNK activation and was also required for the interaction with TNF receptor-associated factor (TRAF) 2 and TRAF5, both of which have been implicated in NF-κB activation by members of the TNF-R superfamily. Co-transfection of a dominant negative TRAF2 or TRAF5 blocked NF-κB and SAPK/JNK activation induced by CD27. Recently, a TRAF2-interacting kinase has been identified, termed NF-κB-inducing kinase (NIK). A kinase-inactive mutant NIK blocked CD27-, TRAF2-, and TRAF5-mediated NF-κB and SAPK/JNK activation. These results indicate that TRAF2 and TRAF5 are involved in NF-κB and SAPK/JNK activation by CD27, and NIK is a common downstream kinase of TRAF2 and TRAF5 for NF-κB and SAPK/JNK activation.
FEBS Letters | 1998
Isabelle Carpentier; Wim Declercq; Nikolai Malinin; David Wallach; Walter Fiers; Rudi Beyaert
We previously demonstrated that p38 MAPK is a crucial mediator in the NF‐κB‐dependent gene activation induced by TNF. Here, we have studied the role of several TNF receptor‐associated proteins and caspases in p38 MAPK activation by TNF. The latter appears to be dependent on TRAF2, but independent of FADD or caspases. Remarkably, p38 MAPK activation by TNF proceeds independently of the TRAF2‐associated NF‐κB‐inducing kinase NIK, which is known to bind and activate two recently identified IκB kinases. These results demonstrate that two kinase pathways involved in NF‐κB regulation, viz. NIK and p38 MAPK‐mediated, diverge at the level of TRAF2.
Current Opinion in Immunology | 1998
David Wallach; Mark Boldin; Andrei Kovalenko; Nikolai Malinin; Igor Mett; Jacques Camonis
The yeast two-hybrid technique provides a general approach for cloning cDNAs merely by exploiting the ability of their encoded proteins to bind to a protein of interest. The technique therefore offered a useful access to the analysis of the mechanisms of cell death at the initial stage of their study, when only a few of the proteins involved and very little about their mode of action were known. Conversely, the knowledge of cell death mechanisms gained by this technique provided a useful insight into both the potential and the limitations of this technique.
Annual Review of Immunology | 1999
David Wallach; Eugene Varfolomeev; Nikolai Malinin; Yuri V. Goltsev; and A. V. Kovalenko; Mark Boldin
Nature | 1997
Nikolai Malinin; Mark Boldin; Andrei Kovalenko; David Wallach
Proceedings of the National Academy of Sciences of the United States of America | 1998
Bakary S. Sylla; Siu Chun Hung; David Davidson; Eudoxia G. Hatzivassiliou; Nikolai Malinin; David Wallach; Thomas D. Gilmore; Elliott Kieff; George Mosialos
Archive | 1997
David Wallach; Nikolai Malinin; Mark Boldin; Andrei Kovalenko; Igor Mett
Archive | 1998
David Wallach; Mark Boldiin; Nikolai Malinin
Archive | 1999
David Wallach; Nikolai Malinin; Mark Boldin; Andrei Kovalenko; Igor Mett