NMR uncovers direct interaction between human NEDD4-1 and p34(SEI-1).
Biochem Biophys Res Commun. 2017 Jun 27;:
Authors: Shrestha P, Yun JH, Ko YJ, Yeon KJ, Kim D, Lee H, Jin DH, Nam KY, Yoo HD, Lee W
Abstract
PTEN, an important tumor suppressor and a key regulator of the PI3K/AKT signaling pathway, is often deleted/mutated in different types of cancer. The E3 ubiquitin ligase NEDD4-1 catalyzes the polyubiquitination of PTEN, thereby acting as a negative regulator of PTEN. Stability of NEDD4-1, in turn, is tightly controlled by a 34*kDa oncoprotein, p34(SEI-1) and it regulates PTEN degradation and activates PI3K/AKT pathway, resulting in cancer metastasis. p34(SEI-1) affects not only the expression of NEDD4-1 during transcription and translation but also the subcellular localization of PTEN. This emphasizes the need to understand, at molecular level, the interaction between NEDD4-1 and p34(SEI-1). A recent study showed that NEDD4-1 interacts with p34(SEI-1) via its WWI domain. However, a detailed interaction for molecular level is yet unknown. We report that the WW1 domain of NEDD4-1 recognizes the SERTA domain containing the proline rich region (PRR motif) in p34(SEI-1). TALOS analysis based on NMR data confirms three conserved ?-sheets in NEDD4-1 WW1 and the central ?-sheet of NEDD4-1 WW1 plays a role for protein stability by the backbone dynamics experiments. NMR titration data revealed the binding site for p34(SEI-1) with NEDD4-1. Our data will provide insights into the molecular mechanism of NEDD4-1 and p34(SEI-1) interaction, which will be directly used for drug design which inhibits the molecular interaction involved in different cancer signaling.
PMID: 28666866 [PubMed - as supplied by publisher]
[NMR paper] Direct Determination of Site-specific Noncovalent Interaction Strengths of Proteins from NMR-derived Fast Side Chain Motional Parameters.
Direct Determination of Site-specific Noncovalent Interaction Strengths of Proteins from NMR-derived Fast Side Chain Motional Parameters.
Related Articles Direct Determination of Site-specific Noncovalent Interaction Strengths of Proteins from NMR-derived Fast Side Chain Motional Parameters.
J Phys Chem B. 2017 Apr 28;:
Authors: Tatikonda RR, Krishnan M
Abstract
A novel approach to accurately determine residue-specific noncovalent interaction strengths (?) of proteins from NMR-measured fast side chain motional parameters...
nmrlearner
Journal club
0
04-30-2017 05:31 PM
[NMR paper] Dual screening of BPTF and Brd4 using protein-observed fluorine NMR uncovers new bromodomain probe molecules.
Dual screening of BPTF and Brd4 using protein-observed fluorine NMR uncovers new bromodomain probe molecules.
Dual screening of BPTF and Brd4 using protein-observed fluorine NMR uncovers new bromodomain probe molecules.
ACS Chem Biol. 2015 Jul 9;
Authors: Urick AK, Hawk LM, Cassel MK, Mishra NK, Liu S, Adhikari N, Zhang W, Dos Santos CO, Hall JL, Pomerantz WC
Abstract
Bromodomain-containing protein dysregulation is linked to cancer, diabetes, and inflammation. Selec-tive inhibition of bromodomain function is a newly...
nmrlearner
Journal club
0
07-12-2015 07:12 AM
Metabolomic Study Uncovers Obesity-related Urine Signature - GenomeWeb
<img alt="" height="1" width="1">
Metabolomic Study Uncovers Obesity-related Urine Signature
GenomeWeb
As part of the International Study of Macro- and Micronutrients and Blood Pressure, or INTERMAP, the team used a combination of nuclear magnetic resonance spectroscopy and ion exchange chromatography to track metabolite patterns in urine samples ...
and more »
Metabolomic Study Uncovers Obesity-related Urine Signature - GenomeWeb
More...
nmrlearner
Online News
0
04-30-2015 07:41 AM
[NMR paper] Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network.
Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network.
Related Articles Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network.
J Struct Funct Genomics. 2014 Jun 19;
Authors: Xu X, Pulavarti SV, Eletsky A, Huang YJ, Acton TB, Xiao R, Everett JK, Montelione GT, Szyperski T
Abstract
High-quality...
nmrlearner
Journal club
0
06-20-2014 08:14 PM
[NMR paper] Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates.
Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates.
Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates.
Chemistry. 2013 Aug 12;
Authors: Diana D, Smaldone G, De Antonellis P, Pirone L, Carotenuto M, Alonzi A, Di Gaetano S, Zollo M, Pedone EM, Fattorusso R
Abstract
Get well prune: The C-terminal third domain of h-prune is largely unfolded and involved in relevant protein-protein interactions, particularly with...
nmrlearner
Journal club
0
08-14-2013 05:24 PM
Evidence from NMR interaction studies challenges the hypothesis of direct lipid transfer from L-FABP to malaria sporozoite protein UIS3
Evidence from NMR interaction studies challenges the hypothesis of direct lipid transfer from L-FABP to malaria sporozoite protein UIS3
Abstract
UIS3 is a malaria parasite protein essential for liver stage development of Plasmodium species, presumably localized to the membrane of the parasitophorous vacuole formed in infected cells. It has been recently proposed that the soluble domain of UIS3 interacts with the host liver fatty acid binding protein (L-FABP), providing the parasite with a pathway for importing exogenous lipids required for its rapid growth. This finding may suggest...
nmrlearner
Journal club
0
02-03-2013 09:54 AM
[NMR paper] An NMR study of the interaction between the human copper(I) chaperone and the second
An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
Related Articles An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
FEBS J. 2005 Feb;272(3):865-71
Authors: Banci L, Bertini I, Ciofi-Baffoni S, Chasapis CT, Hadjiliadis N, Rosato A
The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein...
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[NMR paper] NMR studies of tandem WW domains of Nedd4 in complex with a PY motif-containing regio
NMR studies of tandem WW domains of Nedd4 in complex with a PY motif-containing region of the epithelial sodium channel.
Related Articles NMR studies of tandem WW domains of Nedd4 in complex with a PY motif-containing region of the epithelial sodium channel.
Biochem Cell Biol. 1998;76(2-3):341-50
Authors: Kanelis V, Farrow NA, Kay LE, Rotin D, Forman-Kay JD
Nedd4 (neuronal precursor cell-expressed developmentally down-regulated 4) is a ubiquitin-protein ligase containing multiple WW domains. We have previously demonstrated the association...
NMR uncovers direct interaction between human NEDD4-1 and p34(SEI-1).
Linear Mode
