cytoplasmic sequestering of transcription factor

transcription factor binding, cytoplasmic sequestering

The selective interaction of a transcription factor with specific molecules in the cytoplasm, thereby inhibiting its translocation into the nucleus.

The directed movement of creatine into, out of, within or between cells. Creatine is a compound synthesized from the amino acids arginine, glycine, and methionine that occurs in muscle.

A prolongation or process extending from a cell, e.g. a flagellum or axon.

The directed movement of flavin-adenine dinucleotide (FAD) into, out of, within or between cells. FAD forms the coenzyme of the prosthetic group of various flavoprotein oxidoreductase enzymes, in which it functions as an electron acceptor by being reversibly converted to its reduced form.

The directed movement of folic acid (pteroylglutamic acid) into, out of, within or between cells. Folic acid is widely distributed as a member of the vitamin B complex and is essential for the synthesis of purine and pyrimidines.

The directed movement of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, into, out of, within or between cells.

The directed movement of pantothenate into, out of, within or between cells. Pantothenate is the anion of pantothenic acid, the amide of beta-alanine and pantoic acid; it is a B complex vitamin that is a constituent of coenzyme A and is distributed ubiquitously in foods.

The directed movement of thiamin into, out of, within or between cells. Thiamin is vitamin B1, a water soluble vitamin present in fresh vegetables and meats, especially liver.

The directed movement of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom, into, out of or within a cell.

The chemical reactions involving formaldehyde (methanal, H2C=O), a colorless liquid or gas with a pungent odor, commonly used as a fixative or an antibacterial agent.

Interacting selectively with a filamin, any member of a family of high molecular mass cytoskeletal proteins that crosslink actin filaments to form networks and stress fibers. Filamins contain an amino-terminal alpha-actinin-like actin binding domain, which is followed by a rod-domain composed of 4 to 24 100-residue repetitive segments including a carboxy-terminal dimerization domain.