Combining with inositol-1,4,5-triphosphate to initiate a change in cell activity.

A stable complex of seven subunits, two actin-related proteins, Arp2 and Arp3, and five novel proteins (ARPC1-5). Functions in the nucleation of actin filaments.

The joining of 2 or more lipid bilayer membranes that surround a cell.

The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

Interacting selectively with 5S ribosomal RNA, the smallest RNA constituent of a ribosome.

Penetrating at least one phospholipid bilayer of a plasma membrane. Also refers to the state of being buried in the bilayer with no exposure outside the bilayer.

purinergic nucleotide receptor activity, G-protein coupled

purinergic nucleotide receptor activity, G protein coupled

The chemical reactions involving heterocyclic compounds, those with a cyclic molecular structure and at least two different atoms in the ring (or rings).

The chemical reactions involving ether lipids, lipids that contain (normally) one fatty alcohol in ether linkage to one of the carbon atoms (normally C-1) of glycerol.

The chemical reactions involving glycerolipids, any lipid with a glycerol backbone. Diacylglycerol and phosphatidate are key lipid intermediates of glycerolipid biosynthesis.

The chemical reactions involving glyoxylate, the anion of glyoxylic acid, HOC-COOH.

The chemical reactions involving phosphatidylinositol, any glycophospholipid with its sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.

The initial step in the formation of an actin filament, in which actin monomers combine to form a new filament. Nucleation is slow relative to the subsequent addition of more monomers to extend the filament.

The formation from simpler components of phosphoinositides, any of a class of glycerophospholipids in which the phosphatidyl group is esterified to the hydroxyl group of inositol.

Any complex that includes a dimer of molecules from the kinesin superfamily, a group of related proteins that contain an extended region of predicted alpha-helical coiled coil in the main chain that likely produces dimerization. The native complexes of several kinesin family members have also been shown to contain additional peptides, often designated light chains as all of the noncatalytic subunits that are currently known are smaller than the chain that contains the motor unit. Kinesin complexes generally possess a force-generating enzymatic activity, or motor, which converts the free energy of the gamma phosphate bond of ATP into mechanical work.