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In addition, intracellular accumulation of hyperphosphorlyated tau protein which form neurofibrillary tangle (NFT) is associated with progressive neuronal injury and the development of AD. A\u03b2 and NFTs interact together to induce inflammation and oxidative stress which further induce neurodegeneration in AD. The exact relationship between A\u03b2 and tau, the two proteins that accumulate within these lesions, has proven elusive. A growing body of work supports the notion that A\u03b2 may directly or indirectly interact with tau to accelerate NFTs formation. A\u03b2 can adversely affect distinct molecular and cellular pathways, thereby facilitating tau phosphorylation, aggregation, mislocalization, and accumulation. A\u03b2 may drive tau pathology by activating specific kinases, providing a straightforward mechanism by which A\u03b2 may enhance tau hyperphosphorylation and NFT formation. Many cellular signaling pathways such as protein phosphatase 2A (PP2A), glycogen synthase kinase 3\u03b2 (GSK3\u03b2), and phosphatase and tensin homologue (PTEN) are intricate in AD neuropathology. PP2A which involved in the dephosphorylation of tau protein is deregulated in AD, and correlated with cognitive impairment. PTEN is a critical regulator of neuronal growth, survival, and development, improving synaptic plasticity and axonal regeneration. Nevertheless, mutated PTEN is associated with the development of cognitive impairment by inhibiting the expression and the activity of PP2A. Furthermore, dysregulation of GSK3\u03b2 affects A\u03b2, tau protein phosphorylation, synaptic plasticity and other signaling pathways involved in the pathogenesis of AD. Therefore, there is a close interaction among GSK3\u03b2, PTEN, and PP2A. GSK3\u03b2 exaggerates AD neuropathology by inhibiting PP2A and activates the expression of PTEN. These findings specified a related interaction among GSK3\u03b2, PTEN, and PP2A, and modulation of the single component of this axis may not produce an effective effect against AD neuropathology. Modulation of this axis by metformin and statins can reduce AD neuropathology. Therefore, this review aims to discuss the role of GSK3\u03b2\/PTEN\/PP2A axis in AD neuropathology and how targeting of this axis by metformin and statins can produce effective therapeutic strategy in the management of AD. In conclusion, inhibition of GSK3\u03b2 and PTEN and activation of PP2A may be more suitable than modulation of single signaling pathway. Metformin and statins by activating PP2A and inhibiting of GSK3\u03b2 and PTEN attenuate the development and progression of AD.<\/jats:p>\n                  <jats:p>\n                    <jats:bold>Graphical Abstract<\/jats:bold>\n                  <\/jats:p>","DOI":"10.1007\/s10571-025-01554-0","type":"journal-article","created":{"date-parts":[[2025,4,18]],"date-time":"2025-04-18T14:28:21Z","timestamp":1744986501000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Targeting of PP2 A\/GSK3\u03b2\/PTEN Axis in Alzheimer Disease: The Mooting Evidence, Divine, and Devil"],"prefix":"10.1007","volume":"45","author":[{"given":"Saad Misfer","family":"Alqahtani","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hayder M.","family":"Al-Kuraishy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ali I.","family":"Al-Gareeb","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9019-8932","authenticated-orcid":false,"given":"Maha M.","family":"Abdel-Fattah","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ahad Amer","family":"Alsaiari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mubarak","family":"Alruwaili","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9020-874X","authenticated-orcid":false,"given":"Marios","family":"Papadakis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Athanasios","family":"Alexiou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7817-425X","authenticated-orcid":false,"given":"Gaber El-Saber","family":"Batiha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,4,18]]},"reference":[{"key":"1554_CR1","doi-asserted-by":"publisher","first-page":"2622","DOI":"10.1007\/s12035-016-9839-9","volume":"54","author":"T Ahmed","year":"2017","unstructured":"Ahmed T, Javed S, Javed S, Tariq A, \u0160amec D, Tejada S, Nabavi SF, Braidy N, Nabavi SM (2017) Resveratrol and Alzheimer\u2019s disease: mechanistic insights. 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