The ring-forming molecular chaperone Hsp104/ClpB is a member of the AAA+ protein family which rescues proteins from aggregated states. The newly determined crystal structure of ClpB provides new insights into the mechanism of protein disaggregation, suggesting a crowbar activity mediated by a unique coiled-coil domain.

Oxazolidinone is a five-member heterocyclic ring exhibiting potential medicinal properties with preferential antibacterial activity. Scientists reported various synthetic procedures for this heterocyclic structure. Current review articles tried to cover each and every potential aspect of oxazolidinone like synthetic routes, pharmacological mechanism of action, medicinal properties, and current ...

We and others recently discovered HHLA2 as a new B7 family member and transmembrane and immunoglobulin domain containing 2 (TMIGD2) as one of its receptors. Based on a new study we propose that HHLA2 may represent a novel immunosuppressive mechanism within the tumor microenvironment and hence could be a target for cancer therapy. TMIGD2 may be another therapeutic target.

Malfunction of cystic fibrosis transmembrane conductance regulator (CFTR), a member of the ABC protein superfamily that functions as an ATP-gated chloride channel, causes the lethal genetic disease, cystic fibrosis. This review focuses on the most recent findings on the gating mechanism of CFTR. Potential clinical relevance and implications to ABC transporter function are also discussed.

Defects in the mitochondrial AAA protease family member, paraplegin, result in an autosomal recessive form of hereditary spastic paraplegia (HSP). In this issue of Cell, Nolden et al. (2005) report a new molecular mechanism for HSP based on the requirement of paraplegin for the proteolysis of a specific mitochondrial ribosomal protein. The processing of this substrate is required for robust tra...

Purpose: Sirtuins play an important role in cancer development. Sirt7, as a member of this family, is frequently overexpressed in certain carcinomas, but the oncogenic mechanism is seldom reported. In this study, Sirt7 was characterized for its role in colorectal cancer aggressiveness and underlying molecular

The plasma membrane receptor natural killer group 2 member D (NKG2D) underpins a major mechanism whereby natural killer (NK) and T cells recognize malignant cells. We have recently demonstrated that the epithelial-to-mesenchymal transition, one of the first steps of metastatic dissemination, is under the control of an immunological checkpoint that relies on NKG2D-mediated immune responses.

Plasminogen activator inhibitor 1 (PAI-1) inhibits plasminogen activators (u-PA and t-PA) by forming stable complexes endocytosed via a low-density lipoprotein receptor superfamily member-dependent mechanism. PAI-1 circulates actively in plasma and latently in platelets but is also secreted and deposited into the matrix by several cells, where it participates in tissue repair processes.

The spindle position checkpoint (SPOC) is a regulatory mechanism that ensures accurate segregation of chromosomes in polarized cells during mitosis. In this issue of Genes & Development, Chan and Amon (pp. 1639-1649) identify a phosphoprotein phosphatase (Rts1-PP2A) as a new member of the checkpoint in budding yeast and define its role in interpreting spatial information during mitosis.

ISSUE A novel mechanism of action has recently been described for levetiracetam, a member of a new class of anticonvulsants. Levetiracetam binds selectively and with high affinity to a synaptic vesicle protein known as SV2A, thought to be involved with synaptic vesicle exocytosis and presynaptic neurotransmitter release.