Microtubule-associated protein (MAP) and tubulin (MAP and tubulin)

Microtubule-associated proteins (MAPs) are a diverse family of proteins that bind to microtubules, which are dynamic cylindrical polymers assembled from α- and β-tubulin heterodimers[1][4]. Tubulin itself is the structural subunit of microtubules, with γ-tubulin playing a key role in microtubule nucleation[4][5]. MAPs regulate microtubule stability, dynamics, and organization, and are critical for mitosis, intracellular transport, and neuronal differentiation and maintenance[1][3][4]. Tubulin and MAPs are validated therapeutic targets in oncology (targeted by drugs like paclitaxel and vinca alkaloids) and are implicated in neurodegeneration, with alterations in tau protein (a major neuronal MAP) associated with Alzheimer’s disease[1][3][5]. Dysregulation of tubulin isotypes and modifications are associated with cancer drug resistance and neurodevelopmental disorders[5]. As this entry includes both "microtubule-associated proteins" (a large, heterogeneous group—often subclassified) and "tubulin" (a specific protein family), the query is overly broad and would ideally be separated into more specific canonical entities. Note: The target name "Microtubule-associated proteins and tubulin" is overly broad, encompassing an entire interacting system rather than a single gene/protein. For structured databases, MAPs and tubulin (e.g., α-tubulin, β-tubulin, γ-tubulin, tau protein) are typically annotated separately.

Other names

MAPtubulinmicrotubule-associated proteinsα-tubulinbeta-tubulingamma-tubulin

Microtubule stabilization (inhibits depolymerization—e.g., paclitaxel) Microtubule destabilization (inhibits polymerization—e.g., vincristine, colchicine) Inhibition of mitosis/cell division Induction of apoptosis via mitotic arrest