Astrocytes play a crucial role in the clearance of protein aggregates in neurodegenerative disorders. While microglia are primarily responsible for removing extracellular aggregates, astrocytes also contribute significantly. This review discusses the mechanisms by which astrocytes recognize, collect, internalize, and digest extracellular protein aggregates, focusing on α-Synuclein and Tau, two key amyloidogenic proteins involved in neurodegenerative diseases such as Alzheimer's, Parkinson's, and Tauopathies. The review highlights the potential of targeting astrocyte-mediated clearance as a therapeutic strategy for these disorders. Amyloidogenic proteins, such as α-Syn and Tau, misfold and aggregate, leading to the formation of toxic deposits. These aggregates can spread between cells and contribute to disease progression. Astrocytes have been shown to internalize and digest these aggregates through various mechanisms, including phagocytosis, pinocytosis, and macropinocytosis. Receptors such as TLRs, LRP1, and AXL are involved in the recognition and internalization of these aggregates. However, the efficiency of astrocytic clearance can be compromised by the accumulation of aggregates, leading to mitochondrial damage and impaired astrocytic function. The clearance of protein aggregates by astrocytes is a complex process involving multiple pathways and receptors. While astrocytes can effectively remove aggregates, excessive accumulation can lead to pro-inflammatory responses and impair their ability to support neuronal function. The role of astrocytes in neurodegenerative diseases is still debated, with some studies suggesting they may contribute to disease progression, while others indicate they play a protective role. Understanding the mechanisms of astrocytic clearance is essential for developing targeted therapies to treat neurodegenerative disorders.Astrocytes play a crucial role in the clearance of protein aggregates in neurodegenerative disorders. While microglia are primarily responsible for removing extracellular aggregates, astrocytes also contribute significantly. This review discusses the mechanisms by which astrocytes recognize, collect, internalize, and digest extracellular protein aggregates, focusing on α-Synuclein and Tau, two key amyloidogenic proteins involved in neurodegenerative diseases such as Alzheimer's, Parkinson's, and Tauopathies. The review highlights the potential of targeting astrocyte-mediated clearance as a therapeutic strategy for these disorders. Amyloidogenic proteins, such as α-Syn and Tau, misfold and aggregate, leading to the formation of toxic deposits. These aggregates can spread between cells and contribute to disease progression. Astrocytes have been shown to internalize and digest these aggregates through various mechanisms, including phagocytosis, pinocytosis, and macropinocytosis. Receptors such as TLRs, LRP1, and AXL are involved in the recognition and internalization of these aggregates. However, the efficiency of astrocytic clearance can be compromised by the accumulation of aggregates, leading to mitochondrial damage and impaired astrocytic function. The clearance of protein aggregates by astrocytes is a complex process involving multiple pathways and receptors. While astrocytes can effectively remove aggregates, excessive accumulation can lead to pro-inflammatory responses and impair their ability to support neuronal function. The role of astrocytes in neurodegenerative diseases is still debated, with some studies suggesting they may contribute to disease progression, while others indicate they play a protective role. Understanding the mechanisms of astrocytic clearance is essential for developing targeted therapies to treat neurodegenerative disorders.