Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane.

Defects in plasma membrane repair can lead to muscle and heart diseases in humans. Tripartite motif-containing protein (TRIM)72 (mitsugumin 53; MG53) has been determined to rapidly nucleate vesicles at the site of membrane damage, but the underlying molecular mechanisms remain poorly understood. Here we present the structure of Mus musculus TRIM72, a complete model of a TRIM E3 ubiquitin ligase.

A phage protein-derived antipathogenic peptide that targets type IV pilus assembly.

Phage-inspired antibacterial discovery is a new approach that recruits phages in search for antibacterials with new molecular targets, in that phages are the biological entities well adapted to hijack host bacterial physiology in favor of their own thrive. We previously observed that phage-mediated twitching motility inhibition was effective to control the acute infections caused by and that the motility inhibition was attributed to the delocalization of PilB, the type IV pilus (TFP) assembly ATPase by binding of the 136-amino acid (aa) phage protein, Tip. Here, we created a series of truncated and point-mutant Tip proteins to identify the critical residues in the Tip bioactivity: N-terminal 80-aa residues were dispensable for the Tip activity; we identified that Asp82, Leu84, and Arg85 are crucial in the Tip function.

RACK-1, a receptor for activated C kinase, interacts with the transcription factor NFAT and represses its transactivation.

To isolate and characterize a novel protein that interacts with nuclear factor of activated T cells (NFAT) and potentially regulates its activity, we screened a Jurkat cDNA library by using the NFAT regulatory domain as bait in the yeast two-hybrid system. RACK-1, a receptor for activated protein kinase C and a homologue of the G-protein beta subunit, was identified as a NFAT-binding protein. Mammalian two hybrid tests in CV-1 cells and a coimmunoprecipitation assay confirmed protein-protein interaction between NFAT and RACK-1.

Molecular mechanism of NFAT family proteins for differential regulation of the IL-2 and TNF-alpha promoters.

Nuclear factor of activated T cells (NFAT) is a family of transcription factors that regulates activation-induced transcription of many immunologically important genes. Although all NFAT family proteins contain a highly conserved DNA-binding domain and also bind cooperatively with AP-1 proteins to the interleukin-2 (IL-2) promoter NFAT site, each member shows characteristic site preferences to other promoters. Previously, we have shown that NFATc.