hpa002044

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The 26S proteasome: subunits and functions.

K Tanaka et al.

Molecular biology reports, 24(1-2), 3-11 (1997-03-01)

The 26S proteasome is an eukaryotic ATP-dependent, dumbbell-shaped protease complex with a molecular mass of approximately 2000 kDa. It consists of a central 20S proteasome, functioning as a catalytic machine, and two large V-shaped terminal modules, having possible regulatory roles

C9orf72 FTLD/ALS-associated Gly-Ala dipeptide repeat proteins cause neuronal toxicity and Unc119 sequestration.

Stephanie May et al.

Acta neuropathologica, 128(4), 485-503 (2014-08-15)

Hexanucleotide repeat expansion in C9orf72 is the most common pathogenic mutation in patients with amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Despite the lack of an ATG start codon, the repeat expansion is translated in all reading frames

Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases.

Yoon Park et al.

Molecular and cellular biology, 25(9), 3842-3853 (2005-04-16)

The 26S proteasome, composed of the 20S core and the 19S regulatory complex, plays a central role in ubiquitin-dependent proteolysis by catalyzing degradation of polyubiquitinated proteins. In a search for proteins involved in regulation of the proteasome, we affinity purified

Rtp801 suppression of epithelial mTORC1 augments endotoxin-induced lung inflammation.

Aaron M Nadon et al.

The American journal of pathology, 184(9), 2382-2389 (2014-07-13)

The mechanistic target of rapamycin (mTOR) is a central regulator of cellular responses to environmental stress. mTOR (and its primary complex mTORC1) is, therefore, ideally positioned to regulate lung inflammatory responses to an environmental insult, a function directly relevant to

Differential expression of novel tyrosine kinase substrates during breast cancer development.

Yunhao Chen et al.

Molecular & cellular proteomics : MCP, 6(12), 2072-2087 (2007-09-15)

To identify novel tyrosine kinase substrates that have never been implicated in cancer, we studied the phosphoproteomic changes in the MCF10AT model of breast cancer progression using a combination of phosphotyrosyl affinity enrichment, iTRAQ technology, and LC-MS/MS. Using complementary MALDI-

Salinomycin suppresses LRP6 expression and inhibits both Wnt/β-catenin and mTORC1 signaling in breast and prostate cancer cells.

Wenyan Lu et al.

Journal of cellular biochemistry, 115(10), 1799-1807 (2014-06-07)

Emerging evidence indicates that activation of Wnt/β-catenin signaling at the cell surface results in inhibition of glycogen synthase kinase 3β (GSK3β), leading to activation of mTORC1 signaling in cancer cells. The low density lipoprotein receptor-related protein-6 (LRP6) is an essential

Chromosomal localization and immunological analysis of a family of human 26S proteasomal ATPases.

N Tanahashi et al.

Biochemical and biophysical research communications, 243(1), 229-232 (1998-02-25)

The 26S proteasome is a eukaryotic ATP-dependent protease functioning as a protein death machine. It is a large multisubunit complex, consisting of a catalytic 20S proteasome and two regulatory modules, named PA700. The PA700 complex is composed of multiple subunits

A component of the 26S proteasome binds on orphan member of the nuclear hormone receptor superfamily.

H S Choi et al.

The Journal of steroid biochemistry and molecular biology, 56(1-6 Spec No), 23-30 (1996-01-01)

The 26S proteasome complex plays a general role in turnover of both short and long lived proteins by specifically degrading ubiquitinated proteins. Recent evidence suggests that this large protease has more specific functions in a number of important cellular processes

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