PostTranslationalmodifikationen

Posttranslationalmodifikationen, often abbreviated as PTMs, are chemical changes that occur to a protein after its translation from messenger RNA. These modifications play a crucial role in expanding the functional diversity of the proteome, as a single gene can give rise to multiple protein variants with distinct properties and functions. PTMs can affect a protein's structure, stability, localization, interactions with other molecules, and overall biological activity.

The repertoire of PTMs is extensive and includes a wide array of biochemical alterations. Some of the most common modifications include phosphorylation, the addition of a phosphate group, which is a key regulatory mechanism in signal transduction pathways. Glycosylation, the attachment of carbohydrate chains, influences protein folding, stability, and cell-cell recognition. Ubiquitination, the covalent attachment of ubiquitin, a small protein, often targets proteins for degradation but can also mediate other cellular processes. Other significant PTMs include acetylation, methylation, and lipidation.

PTMs are dynamic and reversible in many cases, allowing cells to respond rapidly to environmental changes and internal signals. The precise pattern of PTMs on a protein, known as the "covalentome," is critical for its proper function. Dysregulation of PTMs is implicated in a variety of diseases, including cancer, neurodegenerative disorders, and metabolic diseases, making the study of PTMs a vital area of research in molecular biology and medicine.