mikrotubulidynamikhämmare

Mikrotubulidyn is not a widely established term in current biology. It may represent a truncated or misspelled reference to microtubule dynamics or to proteins that regulate them. This article provides a concise overview of microtubule dynamics as understood in eukaryotic cells. Microtubules are hollow filaments composed of α- and β-tubulin dimers that assemble into hollow tubes. They exhibit dynamic instability, with phases of growth and rapid shrinkage driven by GTP hydrolysis on β-tubulin. The plus end typically grows and shrinks more rapidly than the minus end, contributing to rapid remodeling of cellular architecture. Critical for function are microtubule-associated proteins and regulators that modulate polymerization, catastrophe frequency, rescue, and stability. Examples include XMAP215/CH-TOG family proteins that promote growth, CLASP proteins that stabilize microtubules, and end-binding proteins that track the growing plus end. Stathmin/Op18 sequesters tubulin dimers and dampens polymerization. Motor proteins such as dynein and several kinesins move cargo along microtubules and participate in spindle dynamics during cell division. Microtubule behavior is essential for mitosis, intracellular transport, and cell polarity. Disruption of microtubule dynamics is implicated in cancer, neurodegenerative diseases, and developmental disorders. Researchers observe microtubule behavior using fluorescence microscopy, live-cell imaging, and biophysical assays to measure growth rates, shrinkage, and rescue frequencies.