Tubulin polymerization-promoting protein (TPPP) family (TPPP)

The Tubulin polymerization-promoting protein family (TPPP) consists of several structurally related proteins that regulate the assembly and stability of microtubules by promoting tubulin polymerization and inducing bundling. The best-characterized member is TPPP/p25, which is highly expressed in neural tissue where it stabilizes myelin sheaths and accumulates abnormally in Lewy bodies characteristic of Parkinson's disease. Other members include TPPP2, involved primarily in spermiogenesis and sperm motility, without strong evidence for direct involvement in neuronal pathology. These proteins do not form part of the structural α-, β-, γ-, δ-, ε-tubulins but instead modulate their function through dynamic interactions at both molecular and cellular levels. Dysfunctional regulation by these proteins has been implicated mainly in neurodegeneration and reproductive disorders but could have broader implications given their central role in maintaining cytoskeletal integrity[3][5][7][9]. If you need structured information about individual *α-/β-/γ-tubulins* themselves rather than regulatory MAPs like *TPPP*, please clarify your request accordingly—they represent different molecular families within cell biology.

Other names

TPPPTubulin Polymerization Promoting Proteinp25 (for a specific brain-enriched member)TPPP2TPPP3

For hypothetical drugs targeting this molecule: - Inhibition or modulation of microtubule assembly/disassembly via interference with tubulin binding or bundling activity. - Modulation of post-translational modifications affecting interaction with other cytoskeletal elements. *Note:* Existing anti-microtubule agents act directly on α/β-tubulins rather than on regulatory MAPs like TPPPs.