Protein Interaction Domains and Motifs

Publication Title: 
PloS One

Mutations in the fused in sarcoma/translated in liposarcoma gene (FUS/TLS, FUS) have been identified in sporadic and familial forms of amyotrophic lateral sclerosis (ALS). FUS is an RNA-binding protein that is normally localized in the nucleus, but is mislocalized to the cytoplasm in ALS, and comprises cytoplasmic inclusions in ALS-affected areas. However, it is still unknown whether the neurodegeneration that occurs in ALS is caused by the loss of FUS nuclear function, or by the gain of toxic function due to cytoplasmic FUS aggregation.

Author(s): 
Sasayama, Hiroshi
Shimamura, Mai
Tokuda, Takahiko
Azuma, Yumiko
Yoshida, Tomokatsu
Mizuno, Toshiki
Nakagawa, Masanori
Fujikake, Nobuhiro
Nagai, Yoshitaka
Yamaguchi, Masamitsu
Publication Title: 
Nucleic Acids Research

The eukaryotic DNA replication initiation factor Mcm10 is essential for both replisome assembly and function. Human Mcm10 has two DNA-binding domains, the conserved internal domain (ID) and the C-terminal domain (CTD), which is specific to metazoans. SIRT1 is a nicotinamide adenine dinucleotide (NAD)-dependent deacetylase that belongs to the sirtuin family. It is conserved from yeast to human and participates in cellular controls of metabolism, longevity, gene expression and genomic stability.

Author(s): 
Fatoba, Samuel T.
Tognetti, Silvia
Berto, Melissa
Leo, Elisabetta
Mulvey, Claire M.
Godovac-Zimmermann, Jasminka
Pommier, Yves
Okorokov, Andrei L.
Publication Title: 
Cell Cycle (Georgetown, Tex.)

Cellular quiescence is a reversible cell cycle arrest that is poised to re-enter the cell cycle in response to a combination of cell-intrinsic factors and environmental cues. In hematopoietic stem cells, a coordinated balance between quiescence and differentiating proliferation ensures longevity and prevents both genetic damage and stem cell exhaustion. However, little is known about how all these processes are integrated at the molecular level.

Author(s): 
Yamada, Takeshi
Park, Chun Shik
Lacorazza, H. Daniel
Publication Title: 
Epigenetics

DNA methylation is an epigenetic mark that is essential for the development of mammals; it is frequently altered in diseases ranging from cancer to psychiatric disorders. The presence of DNA methylation attracts specialized methyl-DNA binding factors that can then recruit chromatin modifiers. These methyl-CpG binding proteins (MBPs) have key biological roles and can be classified into three structural families: methyl-CpG binding domain (MBD), zinc finger, and SET and RING finger-associated (SRA) domain.

Author(s): 
Buck-Koehntop, Bethany A.
Defossez, Pierre-Antoine
Publication Title: 
The American Journal of Clinical Hypnosis

This paean composed on the occasion of the inaugural Bernauer W. Newton Trust presentation celebrates the personal and professional culture of 50 years of mentorship, teaching, and research by the American Society for Clinical Hypnosis (ASCH). This review of current neuroscience concepts of therapeutic hypnosis and psychotherapy is made possible by the cooperation and dedication of all members of our society.

Author(s): 
Rossi, Ernest Lawrence
Publication Title: 
The Journal of Biological Chemistry

Our recent study has shown that betaA3-crystallin along with betaB1- and betaB2-crystallins were part of high molecular weight complex obtained from young, old, and cataractous lenses suggesting potential interactions between alpha- and beta-crystallins (Srivastava, O. P., Srivastava, K., and Chaves, J. M. (2008) Mol. Vis. 14, 1872-1885). To investigate this further, this study was carried out to determine the interaction sites of betaA3-crystallin with alphaA- and alphaB-crystallins.

Author(s): 
Gupta, Ratna
Srivastava, Om P.
Publication Title: 
The Journal of Biological Chemistry

Protein-tyrosine phosphatase 1B (PTP1B) is a physiological regulator of glucose homeostasis and adiposity and is a drug target for the treatment of obesity and diabetes. Here we identify pyruvate kinase M2 (PKM2) as a novel PTP1B substrate in adipocytes. PTP1B deficiency leads to increased PKM2 total tyrosine and Tyr(105) phosphorylation in cultured adipocytes and in vivo. Substrate trapping and mutagenesis studies identify PKM2 Tyr-105 and Tyr-148 as key sites that mediate PTP1B-PKM2 interaction.

Author(s): 
Bettaieb, Ahmed
Bakke, Jesse
Nagata, Naoto
Matsuo, Kosuke
Xi, Yannan
Liu, Siming
AbouBechara, Daniel
Melhem, Ramzi
Stanhope, Kimber
Cummings, Bethany
Graham, James
Bremer, Andrew
Zhang, Sheng
Lyssiotis, Costas A.
Zhang, Zhong-Yin
Cantley, Lewis C.
Havel, Peter J.
Haj, Fawaz G.
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