scholarly journals Receptor Interacting Protein Kinase-Mediated Necrosis Contributes to Cone and Rod Photoreceptor Degeneration in the Retina Lacking Interphotoreceptor Retinoid-Binding Protein

2013 ◽  
Vol 33 (44) ◽  
pp. 17458-17468 ◽  
Author(s):  
K. Sato ◽  
S. Li ◽  
W. C. Gordon ◽  
J. He ◽  
G. I. Liou ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Binding Protein ◽  
Rod Photoreceptor ◽  
Photoreceptor Degeneration ◽  
Interacting Protein ◽  
Interphotoreceptor Retinoid Binding Protein

scholarly journals Critical role of X-box binding protein 1 in NADPH oxidase 4-triggered cardiac hypertrophy is mediated by receptor interacting protein kinase 1

Cell Cycle ◽  
2017 ◽  
Vol 16 (4) ◽  
pp. 348-359 ◽  
Author(s):  
Li Chen ◽  
Mingyue Zhao ◽  
Junli Li ◽  
Yu Wang ◽  
Qinxue Bao ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Nadph Oxidase ◽  
Cardiac Hypertrophy ◽  
Binding Protein ◽  
Critical Role ◽  
Interacting Protein ◽  
Nadph Oxidase 4

scholarly journals Interaction and Cooperation of the CCAAT-box Enhancer-binding Protein β (C/EBPβ) with the Homeodomain-interacting Protein Kinase 2 (Hipk2)

2013 ◽  
Vol 288 (31) ◽  
pp. 22257-22269 ◽  
Author(s):  
Simone Steinmann ◽  
Anna Coulibaly ◽  
Johanna Ohnheiser ◽  
Anke Jakobs ◽  
Karl-Heinz Klempnauer
Keyword(s):  
Protein Kinase ◽  
Binding Protein ◽  
Interacting Protein ◽  
Enhancer Binding Protein ◽  
Ccaat Box

Interphotoreceptor Retinoid-Binding Protein: A Link Between Retinal Rod Photoreceptor Cells and Pineal Gland

1986 ◽  
pp. 363-382
Author(s):  
Gerald J. Chader ◽  
Barbara Wiggert ◽  
Igal Gery ◽  
Ling Lee ◽  
T. Michael Redmond ◽  
...  
Keyword(s):  
Pineal Gland ◽  
Binding Protein ◽  
Protein A ◽  
Photoreceptor Cells ◽  
Rod Photoreceptor ◽  
Interphotoreceptor Retinoid Binding Protein ◽  
Retinal Rod

scholarly journals Regulation of Genotoxic Stress Response by Homeodomain-interacting Protein Kinase 2 through Phosphorylation of Cyclic AMP Response Element-binding Protein at Serine 271

2010 ◽  
Vol 21 (16) ◽  
pp. 2966-2974 ◽  
Author(s):  
Kensuke Sakamoto ◽  
Bo-Wen Huang ◽  
Kenta Iwasaki ◽  
Kiros Hailemariam ◽  
Jun Ninomiya-Tsuji ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Mrna Expression ◽  
Binding Protein ◽  
Genotoxic Stress ◽  
Bdnf Mrna ◽  
Interacting Protein ◽  
Element Binding Protein ◽  
Cyclic Amp Response Element ◽  
Creb Kinase

CREB (cyclic AMP response element-binding protein) is a stimulus-induced transcription factor that plays pivotal roles in cell survival and proliferation. The transactivation function of CREB is primarily regulated through Ser-133 phosphorylation by cAMP-dependent protein kinase A (PKA) and related kinases. Here we found that homeodomain-interacting protein kinase 2 (HIPK2), a DNA-damage responsive nuclear kinase, is a new CREB kinase for phosphorylation at Ser-271 but not Ser-133, and activates CREB transactivation function including brain-derived neurotrophic factor (BDNF) mRNA expression. Ser-271 to Glu-271 substitution potentiated the CREB transactivation function. ChIP assays in SH-SY5Y neuroblastoma cells demonstrated that CREB Ser-271 phosphorylation by HIPK2 increased recruitment of a transcriptional coactivator CBP (CREB binding protein) without modulation of CREB binding to the BDNF CRE sequence. HIPK2−/− MEF cells were more susceptible to apoptosis induced by etoposide, a DNA-damaging agent, than HIPK2+/+ cells. Etoposide activated CRE-dependent transcription in HIPK2+/+ MEF cells but not in HIPK2−/− cells. HIPK2 knockdown in SH-SY5Y cells decreased etoposide-induced BDNF mRNA expression. These results demonstrate that HIPK2 is a new CREB kinase that regulates CREB-dependent transcription in genotoxic stress.

scholarly journals Complex regulation of CREB-binding protein by homeodomain-interacting protein kinase 2

2015 ◽  
Vol 27 (11) ◽  
pp. 2252-2260 ◽  
Author(s):  
Krisztián A. Kovács ◽  
Myriam Steinmann ◽  
Olivier Halfon ◽  
Pierre J. Magistretti ◽  
Jean-René Cardinaux
Keyword(s):  
Protein Kinase ◽  
Binding Protein ◽  
Creb Binding Protein ◽  
Interacting Protein ◽  
Complex Regulation

scholarly journals Interphotoreceptor Retinoid-Binding Protein Is the Physiologically Relevant Carrier That Removes Retinol from Rod Photoreceptor Outer Segments†

Biochemistry ◽  
2007 ◽  
Vol 46 (29) ◽  
pp. 8669-8679 ◽  
Author(s):  
Qingqing Wu ◽  
Lorie R. Blakeley ◽  
M. Carter Cornwall ◽  
Rosalie K. Crouch ◽  
Barbara N. Wiggert ◽  
...  
Keyword(s):  
Binding Protein ◽  
Rod Photoreceptor ◽  
Photoreceptor Outer Segments ◽  
Outer Segments ◽  
Interphotoreceptor Retinoid Binding Protein

scholarly journals Methyl‐CpG‐binding protein 2 is phosphorylated by homeodomain‐interacting protein kinase 2 and contributes to apoptosis

EMBO Reports ◽  
2009 ◽  
Vol 10 (12) ◽  
pp. 1327-1333 ◽  
Author(s):  
Giorgia Bracaglia ◽  
Barbara Conca ◽  
Anna Bergo ◽  
Laura Rusconi ◽  
Zhaolan Zhou ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Binding Protein ◽  
Interacting Protein

Early signalling events of autophagy

2013 ◽  
Vol 55 ◽  
pp. 1-15 ◽  
Author(s):  
Laura E. Gallagher ◽  
Edmond Y.W. Chan
Keyword(s):  
Protein Kinase ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Mammalian Cells ◽  
Mammalian Target Of Rapamycin ◽  
Interacting Protein ◽  
The Core ◽  
Autophagy Gene ◽  
Autophagy Induction ◽  
Cellular Pathways

Autophagy is a conserved cellular degradative process important for cellular homoeostasis and survival. An early committal step during the initiation of autophagy requires the actions of a protein kinase called ATG1 (autophagy gene 1). In mammalian cells, ATG1 is represented by ULK1 (uncoordinated-51-like kinase 1), which relies on its essential regulatory cofactors mATG13, FIP200 (focal adhesion kinase family-interacting protein 200 kDa) and ATG101. Much evidence indicates that mTORC1 [mechanistic (also known as mammalian) target of rapamycin complex 1] signals downstream to the ULK1 complex to negatively regulate autophagy. In this chapter, we discuss our understanding on how the mTORC1–ULK1 signalling axis drives the initial steps of autophagy induction. We conclude with a summary of our growing appreciation of the additional cellular pathways that interconnect with the core mTORC1–ULK1 signalling module.

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