The WW domain of IQGAP1 binds directly to the p110α catalytic subunit of PI 3-kinase

Autor: A. Jane Bardwell, Madhuri Paul, Kiku C. Yoneda, Maria D. Andrade-Ludeña, Oanh T. Nguyen, David A. Fruman, Lee Bardwell

IQGAP1 is a multi-domain cancer-associated protein that serves as a scaffold protein for multiple signaling pathways. Numerous binding partners have been found for the calponin homology, IQ and GAP-related domains in IQGAP1. Identification of a bindi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba74793cccced6d7bde43b779541c4f3
https://doi.org/10.1101/2022.09.24.509339

The WW domain of the scaffolding protein IQGAP1 is neither necessary nor sufficient for binding to the MAPKs ERK1 and ERK2

Autor: Ronak Zebarjedi, Leonila Lagunes, A. Jane Bardwell, Lee Bardwell

Publikováno v: The Journal of biological chemistry, vol 292, iss 21

Mitogen-activated protein kinase (MAPK) scaffold proteins, such as IQ motif containing GTPase activating protein 1 (IQGAP1), are promising targets for novel therapies against cancer and other diseases. Such approaches require accurate information abo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e859a2e4611fd4462c61c416b3585fe
https://pubmed.ncbi.nlm.nih.gov/28396345

Anthrax lethal factor-cleavage products of MAPK (mitogen-activated protein kinase) kinases exhibit reduced binding to their cognate MAPKs

Autor: A. Jane Bardwell, Lee Bardwell, Mahsa Abdollahi

Publikováno v: Bardwell, A J; Abdollahi, M; & Bardwell, Lee. (2004). Anthrax lethal factor-cleavage products of MAPK (mitogen-activated protein kinase) kinases exhibit reduced binding to their cognate MAPKs. Biochemical Journal, 378, 569-577. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/4d29f3jb

Anthrax lethal toxin is the major cause of death in systemic anthrax. Lethal toxin consists of two proteins: protective antigen and LF (lethal factor). Protective antigen binds to a cell-surface receptor and transports LF into the cytosol. LF is a me

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c21ccd8202489855b34354e7b4964603
https://doi.org/10.1042/bj20031382

Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity

Autor: Mahsa Abdollahi, Lee Bardwell, A. Jane Bardwell

Publikováno v: Biochemical Journal. 370:1077-1085

Mitogen-activated protein kinase (MAPK) cascades control gene expression patterns in response to extracellular stimuli. MAPK/ERK (extracellular-signal-regulated kinase) kinases (MEKs) activate MAPKs by phosphorylating them; activated MAPKs, in turn,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::805a42aa24b04c35df7d2da81917c7fa
https://doi.org/10.1042/bj20021806

Specificity of MAP Kinase Signaling in Yeast Differentiation Involves Transient versus Sustained MAPK Activation

Autor: Lee Bardwell, A. Jane Bardwell, Walid Sabbagh, Laura J. Flatauer

Publikováno v: Molecular Cell. 8(3):683-691

Signals transmitted by common components often elicit distinct (yet appropriate) outcomes. In yeast, two developmental options—mating and invasive growth—are both regulated by the same MAP kinase cascade. Specificity has been thought to result fr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f1b8df9225f713ce559f7af23c74882