Phosphoinositides signaling modulates microglial actin remodeling and phagocytosis in Alzheimer’s disease
Open accessAbstract
Alzheimer’s disease is one of the neurodegenerative diseases, characterized by the accumulation of abnormal protein deposits, which disrupts signal transduction in neurons and other glia cells. The pathological protein in neurodegenerative diseases, Tau and amyloid-β contribute to the disrupted microglial signaling pathways, actin cytoskeleton, and cellular receptor expression. The important secondary messenger lipids i.e., phosphatidylinositols are largely affected by protein deposits of amyloid-β in Alzheimer’s disease. Phosphatidylinositols are the product of different phosphatidylinositol kinases and the state of phosphorylation at D3, D4, and D5 positions of inositol ring. Phosphatidylinositol 3,4,5-triphosphate (PI 3, 4, 5-P3) involves in phagocytic cup formation, cell polarization, whereas Phosphatidylinositol 4,5-bisphosphate (PI 4, 5-P2)-mediates the process of phagosomes formation and further its fusion with early endosome.. The necessary activation of actin-binding proteins such as Rac, WAVE complex, and ARP2/3 complex for the actin polymerization in the process of phagocytosis, migration is regulated and maintained by PI 3, 4, 5-P3 and PI 4, 5-P2. The ratio and types of fatty acid intake can influence the intracellular secondary lipid messengers along with the cellular content of phaphatidylcholine and phosphatidylethanolamine. The Amyloid-β deposits and extracellular Tau seeds disrupt phosphatidylinositides level and actin cytoskeletal network that hamper microglial-signaling pathways in AD. We hypothesize that being a lipid species intracellular levels of phosphatidylinositol would be regulated by dietary fatty acids. Further we are interested to understand phosphoinositide-based signaling cascades in phagocytosis and actin remodeling.
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Rac signaling is upstream of the ABI-WAVE complex and regulates actin cytoskeleton remodeling.
“Rac signaling is upstream of the ABI-WAVE complex and regulates actin cytoskeleton remodeling (51, 52).”
From The effect of Abi3 locus deletion on the progression of Alzheimer’s disease-related pathologies (2023) · cites this paper as [51]
The Background sections on microglial migration and phagocytosis link Rac signaling to actin polymerization and remodeling. The passages do not identify an ABI-WAVE complex or place Rac upstream of it; searches for “ABI-WAVE” and “WAVE Rac1 ABI” found no such passage. Page numbers were unavailable in our copy. (LLM, conf=0.85)
Experimental — accuracy not yet measuredThe literature highlights the crucial involvement of ACTR2 and CFL1 in microglial motility.
“the literature also highlights their crucial involvement in microglial motility [18, 20].”
From Enhanced microglial dynamics and a paucity of tau seeding in the amyloid plaque microenvironment contribute to cognitive resilience in Alzheimer’s disease (2024) · cites this paper as [18]
The Background section, “Phosphatidylinositol signaling in microglial migration” (page unavailable), links ARP2/3-mediated actin polymerization to microglial migration, supporting the ACTR2 aspect at the complex level. It does not identify ACTR2 individually or establish a role for CFL1 in microglial motility; searches for CFL1 and cofilin found no such passage. (LLM, conf=0.83)
Experimental — accuracy not yet measuredThe ACTR2 (encoding ARP2) and CFL1 (Cofilin 1) genes play significant roles in actin remodeling, enabling both baseline movement (ruffling or branching) and chemotactic motility (migration).
“The ACTR2 (encoding ARP2) and CFL1 (Cofilin 1) genes play significant roles in actin remodeling, enabling both baseline movement (ruffling or branching) and chemotactic motility (migration) [18, 28, 29].”
From Enhanced microglial dynamics and a paucity of tau seeding in the amyloid plaque microenvironment contribute to cognitive resilience in Alzheimer’s disease (2024) · cites this paper as [18]
The Background sections on phosphatidylinositol signaling in microglial migration and actin remodeling (pages unavailable) link ARP2/3-mediated actin polymerization to membrane ruffling and migration toward chemoattractants. The passages do not identify ACTR2 or describe a role for CFL1/cofilin 1 in those processes, so they support only the ARP2/3 portion of the claim. (LLM, conf=0.85)
Experimental — accuracy not yet measuredSHIP1 is a phosphatase involved in phosphoinositide signaling.
“SHIP1 is a phosphatase involved in phosphoinositide signaling.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [89]
The Background section (‘Phosphatidylinositol influence actin remodeling’; page unavailable) identifies SHIP as an inositol phosphatase and says it hydrolyzes PIP3 to produce a phosphoinositide signaling molecule. Our copy calls it SHIP, not SHIP1, so it does not explicitly establish the claim for that specific isoform. (LLM, conf=0.82)
Experimental — accuracy not yet measuredPI(3,4,5)P3 can be converted back to PI(4,5)P2 by PTEN or converted into PI(3,4)P2 by SHIP1, which negatively regulates PI3K/Akt signaling.
“PI(3,4,5)P3 can be converted back to PI(4,5)P2 by the protein phosphatase and tensin homology (PTEN) or converted into PI(3,4)P2 by SHIP1, which negatively regulates PI3K/Akt signaling (Fig. 2) [89–92].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [89]
The Background section (‘Phosphatidylinositol influence actin remodeling’; page unavailable) states that PTEN converts PI(3,4,5)P3 to PI(4,5)P2 and SHIP converts it to PI(3,4)P2. It does not identify that enzyme specifically as SHIP1 or state that this conversion negatively regulates PI3K/Akt signaling. (LLM, conf=0.87)
Experimental — accuracy not yet measured
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Watanabe, H., Song, T., Choi, J., Lee, M., Choi, K., Kim, J., Sherry, B. A., Diamond, B., Zou, Y.-R., & Son, M. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1588987
Antibodies targeting amyloid-β and Tau oligomers in Alzheimer’s disease
Chinnathambi, S., Rangappa, N., & Chandrashekar, M. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.002
Self-citationZhang, T., & Zhu, H. (2025) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1013697
Tau-Cytoskeleton and their interaction with other neurodegenerative proteins
Sahu, S., Rangappa, N., Chinnathambi, S., & Mishra, M. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.032
Self-citationChinnathambi, S., Rangappa, N., & Chandrashekar, M. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.023
Self-citationCytoskeltal intermediate filaments in Tau pathology and neurodegeneration
Chinnathambi, S., & Malik, S. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.028
Self-citationChinnathambi, S., Suresh, S., Velmurugan, G., & Mishra, A. (2025) · Advances in immunology · doi:10.1016/bs.ai.2025.11.004
Self-citationiPSC-derived neurospheres: A cellular platform for Tau and Alzheimer’s disease immunotherapy
Chinnathambi, S., Adityan, A., Chandrashekar, M., & Velmurugan, G. (2025) · Advances in immunology · doi:10.1016/bs.ai.2025.11.001 · Cited by 1 · see citing works
Self-citationAnanathanarayana, V., Upadhyay, R., Illanad, G. H., Krishnan, D., Bochageri, N. P., Sevanan, M., Bagewadi, Z., Sivasamy, R., & Chinnathambi, S. (2025) · Advances in immunology · doi:10.1016/bs.ai.2025.11.002
Self-citationChidamabram, H., Ananathanarayana, V., & Chinnathambi, S. (2025) · Advances in immunology · doi:10.1016/bs.ai.2025.11.003
Self-citationInduced-pluripotent stem cell-derived immunotherapy for Tau and Alzheimer’s disease
Chinnathambi, S. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.005
Self-citationActin cytoskeletal pathology in Alzheimer’s disease
Chinnathambi, S., Malik, S., Chandrashekar, M., & Rangappa, N. (2026) · Advances in pharmacology · doi:10.1016/bs.apha.2025.12.003
Self-citationPodosomes in Alzheimer’s disease
Malik, S., Velmurugan, G., Mishra, A. K., & Chinnathambi, S. (2026) · Advances in pharmacology · doi:10.1016/bs.apha.2025.12.002
Self-citationLipidomics reveals TREM2-associated dysregulation of plasma lipid metabolism in Alzheimer's disease
Zhang, T., He, M., Wang, Y., Gao, P., Xia, X., Li, J., Yin, Y., 赵国栋, Chen, O., Qu, M., et al. (2026) · Journal of Alzheimer s Disease · doi:10.1177/13872877261450934
Phosphoinositide turnover through PLCγ regulates Draper-dependent engulfment in gliaPreprint
Storer, F., MacKinnon, E. A., Clarke, H., Maddison, D. C., Amadio, L., Susobhanan, T., Malik, B. R., Peters, O. M., & Smith, G. A. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.04.729572
Lüleci̇, H. B., Jones, A., Neff, R. A., Bennett, D. A., Zhang, B., Çakır, T., & Thambisetty, M. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05978-7
Luo, B., Kouznetsova, V. L., & Tsigelny, I. F. (2026) · International Journal of Neural Systems · doi:10.1142/s012906572750002x
Small molecular chaperones regulate protein quality control in neurodegenerative diseases
Rangappa, N., Mishra, A., & Chinnathambi, S. (2026) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2026.06.006
Self-citationCX3CR1-mediated extracellular Tau internalization and phagosomal proteins in iPSC-derived microglia
Narayanappa, T. S., Ananthanarayana, V., & Chinnathambi, S. (2026) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2026.07.011
Self-citationRen, Y., Chen, D., Xie, S., He, Y., Zhuang, X., Ye, D., Fei, Z., Xia, L., Wang, Y., & Li, F. (2026) · Advances in respiratory medicine · doi:10.3390/arm94040054
Reprogramming lipid metabolism in virus-infected neuronal cellsPreprint
Li, L.-Z., Qu, H.-R., Fu, W., & Feng, S. (2026) · Research Square · doi:10.21203/rs.3.rs-10472222/v1
Research Progress of Insulin-like Growth Factor-1 in Major Neurodegenerative Diseases
Sun, Y., & Xia, J. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27219696
- Authors
- Desale, S. E., & Chinnathambi, S.
- Affiliations
- National Chemical Laboratory (IN)
- Corresponding author
- Chinnathambi, Subashchandrabose
- Venue
- Cell Communication and Signaling
- Published
- 2021-02-24
- Volume
- 19
- Issue
- 1
- Pages
- 28-28
- ISSN
- 1478-811X (ISSN-L)
- PMC
- PMC7905611
- OpenAlex
- W3132224281
- Cited by
- 81
- References
- 114
- Citations by year
- 2026: 14 · 2025: 28 · 2024: 18 · 2023: 13 · 2022: 3 · 2021: 5
- FWCI
- 1.30
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Cell Communication and Signaling (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Greater South Information System
- Funders
- Council of Scientific and Industrial Research, India (CSIR NCL MLP029526)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- Alzheimer's disease, microglia, phosphoinositide signaling, actin cytoskeleton remodeling, phagocytosis, phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 4,5-bisphosphate, amyloid-beta, tau protein, actin polymerization, Rac, WAVE complex, Arp2/3 complex, dietary fatty acids, phagosome formation
- MeSH terms
- Actins, Alzheimer Disease, Animals, Humans, Phagocytosis, Phosphatidylinositols, Signal Transduction, Microglia
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