CHIP: a co-chaperone for degradation by the proteasome
- Authors: Edkins, Adrienne L
- Date: 2015
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/164863 , vital:41179 , ISBN 978-3-319-11730-0 , DOI: 10.1007/978-3-319-11731-7_11
- Description: Protein homeostasis relies on a balance between protein folding and protein degradation. Molecular chaperones like Hsp70 and Hsp90 fulfil well-defined roles in protein folding and conformational stability via ATP dependent reaction cycles. These folding cycles are controlled by associations with a cohort of non-client protein co-chaperones, such as Hop, p23 and Aha1. Pro-folding co-chaperones facilitate the transit of the client protein through the chaperone mediated folding process. However, chaperones are also involved in ubiquitin-mediated proteasomal degradation of client proteins. Similar to folding complexes, the ability of chaperones to mediate protein degradation is regulated by co-chaperones, such as the C terminal Hsp70 binding protein (CHIP).
- Full Text:
- Date Issued: 2015
Dynamic mitochondrial localisation of STAT3 in the cellular adipogenesis model 3T3-L1:
- Authors: Kramer, Adam H , Edkins, Adrienne L , Hoppe, Heinrich C , Prinsloo, Earl
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/164885 , vital:41181 , DOI: 10.1002/jcb.25076
- Description: A mechanistic relationship exists between protein localisation, activity and cellular differentiation. Understanding the contribution of these molecular mechanisms is required for elucidation of conditions that drive development. Literature suggests non‐canonical translocation of the Signal Transducer and Activator of Transcription 3 (STAT3) to the mitochondria contributes to the regulation of the electron transport chain, cellular respiration and reactive oxygen species production. Based on this we investigated the role of mitochondrial STAT3, specifically the serine 727 phosphorylated form, in cellular differentiation using the well‐defined mouse adipogenic model 3T3-L1.
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- Date Issued: 2015
Hsp70/Hsp90 organising protein (hop): beyond interactions with chaperones and prion proteins
- Authors: Baindur-Hudson, Swati , Edkins, Adrienne L , Blatch, Gregory L
- Date: 2015
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/164852 , vital:41178 , ISBN 978-3-319-11730-0 , DOI: 10.1007/978-3-319-11731-7_3
- Description: The Hsp70/Hsp90 organising protein (Hop), also known as stress-inducible protein 1 (STI1), has received considerable attention for diverse cellular functions in both healthy and diseased states. There is extensive evidence that intracellular Hop is a co-chaperone of the major chaperones Hsp70 and Hsp90, playing an important role in the productive folding of Hsp90 client proteins. Consequently, Hop is implicated in a number of key signalling pathways, including aberrant pathways leading to cancer. However, Hop is also secreted and it is now well established that Hop also serves as a receptor for the prion protein, PrPC.
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- Date Issued: 2015
The palladacycle, AJ-5, exhibits anti-tumour and anti-cancer stem cell activity in breast cancer cells:
- Authors: Aliwaini, Saeb , Peres, Jade , Kröger, Wendy L , Blanckenberg, Angelique , de la Mare, Jo-Anne , Edkins, Adrienne L , Mapolie, Selwyn , Prince, Sharon
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/164874 , vital:41180 , DOI: 10.1016/j.canlet.2014.11.027
- Description: Breast cancer is the most common malignancy amongst women worldwide but despite enormous efforts to address this problem, there is still limited success with most of the current therapeutic strategies. The current study describes the anti-cancer activity of a binuclear palladacycle complex (AJ-5) in oestrogen receptor positive (MCF7) and oestrogen receptor negative (MDA-MB-231) breast cancer cells as well as human breast cancer stem cells. AJ-5 is shown to induce DNA double strand breaks leading to intrinsic and extrinsic apoptosis and autophagy cell death pathways which are mediated by the p38 MAP kinase. This study provides evidence that AJ-5 is potentially an effective compound in the treatment of breast cancer.
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- Date Issued: 2015