The MNB/DYRK1A protein kinase: Neurobiological functions and Down syndrome implications

2003 ◽  
pp. 129-137 ◽  
Author(s):  
B. Hämmerle ◽  
C. Elizalde ◽  
J. Galceran ◽  
W. Becker ◽  
F. J. Tejedor
Keyword(s):  
Down Syndrome ◽  
Protein Kinase

Protein kinase A phosphorylates Down syndrome critical region 1 (RCAN1)

2012 ◽  
Vol 418 (4) ◽  
pp. 657-661 ◽  
Author(s):  
Seon Sook Kim ◽  
Yohan Oh ◽  
Kwang Chul Chung ◽  
Su Ryeon Seo
Keyword(s):  
Down Syndrome ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Critical Region ◽  
Kinase A

scholarly journals The Down syndrome-related protein kinase DYRK1A phosphorylates p27Kip1and Cyclin D1 and induces cell cycle exit and neuronal differentiation

Cell Cycle ◽  
2014 ◽  
Vol 13 (13) ◽  
pp. 2084-2100 ◽  
Author(s):  
Ulf Soppa ◽  
Julian Schumacher ◽  
Victoria Florencio Ortiz ◽  
Tobias Pasqualon ◽  
Francisco Tejedor ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Down Syndrome ◽  
Protein Kinase ◽  
Cyclin D1 ◽  
Neuronal Differentiation ◽  
Cell Cycle Exit ◽  
Related Protein

A role for the actin cytoskeleton in the hormonal and growth-factor-mediated activation of protein kinase B

2001 ◽  
Vol 353 (3) ◽  
pp. 735
Author(s):  
K. PEYROLLIER ◽  
E. HAJDUCH ◽  
A. GRAY ◽  
G. J. LITHERLAND ◽  
A. R. PRESCOTT ◽  
...  
Keyword(s):  
Growth Factor ◽  
Protein Kinase ◽  
Actin Cytoskeleton ◽  
Protein Kinase B

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.

Spatial control of actin-based motility through plasmalemmal PtdIns(4,5)P2-rich raft assemblies.

2005 ◽  
Vol 72 ◽  
pp. 119-127 ◽  
Author(s):  
Tamara Golub ◽  
Caroni Pico
Keyword(s):  
Protein Kinase ◽  
Cell Surface ◽  
Actin Cytoskeleton ◽  
Lipid Rafts ◽  
Patch Clustering ◽  
Pkc Protein Kinase C ◽  
Membrane Bound ◽  
And Function ◽  
Cytoskeleton Dynamics ◽  
Syndrome Protein

The interactions of cells with their environment involve regulated actin-based motility at defined positions along the cell surface. Sphingolipid- and cholesterol-dependent microdomains (rafts) order proteins at biological membranes, and have been implicated in most signalling processes at the cell surface. Many membrane-bound components that regulate actin cytoskeleton dynamics and cell-surface motility associate with PtdIns(4,5)P2-rich lipid rafts. Although raft integrity is not required for substrate-directed cell spreading, or to initiate signalling for motility, it is a prerequisite for sustained and organized motility. Plasmalemmal rafts redistribute rapidly in response to signals, triggering motility. This process involves the removal of rafts from sites that are not interacting with the substrate, apparently through endocytosis, and a local accumulation at sites of integrin-mediated substrate interactions. PtdIns(4,5)P2-rich lipid rafts can assemble into patches in a process depending on PtdIns(4,5)P2, Cdc42 (cell-division control 42), N-WASP (neural Wiskott-Aldrich syndrome protein) and actin cytoskeleton dynamics. The raft patches are sites of signal-induced actin assembly, and their accumulation locally promotes sustained motility. The patches capture microtubules, which promote patch clustering through PKA (protein kinase A), to steer motility. Raft accumulation at the cell surface, and its coupling to motility are influenced greatly by the expression of intrinsic raft-associated components that associate with the cytosolic leaflet of lipid rafts. Among them, GAP43 (growth-associated protein 43)-like proteins interact with PtdIns(4,5)P2 in a Ca2+/calmodulin and PKC (protein kinase C)-regulated manner, and function as intrinsic determinants of motility and anatomical plasticity. Plasmalemmal PtdIns(4,5)P2-rich raft assemblies thus provide powerful organizational principles for tight spatial and temporal control of signalling in motility.

Auxin induces mitogenic activated protein kinase (MAPK) activation in roots of Arabidopsis seedlings

2000 ◽  
Vol 24 (6) ◽  
pp. 785-796 ◽  
Author(s):  
Keithanne Mockaitis ◽  
Stephen H. Howell
Keyword(s):  
Protein Kinase ◽  
Mapk Activation

The protein kinase Cdk5 Structural aspects, roles in neurogenesis and involvement in Alzheimer's pathology

2001 ◽  
Vol 268 (6) ◽  
pp. 1518-1527 ◽  
Author(s):  
Ricardo B. Maccioni ◽  
Carola Otth ◽  
Ilona I. Concha ◽  
Juan P. Munoz
Keyword(s):  
Protein Kinase ◽  
Alzheimer’S Pathology ◽  
Structural Aspects

Alopecia areata and Down syndrome

1976 ◽  
Vol 112 (10) ◽  
pp. 1397-1399 ◽  
Author(s):  
D. M. Carter
Keyword(s):  
Down Syndrome ◽  
Alopecia Areata
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