Sorting nexin-41 (SNX41/Mug186) is a member of the sorting nexin family containing a PX domain and BAR-superfamily domain. It acts as a membrane adaptor/scaffold (not an enzyme) that couples PI3P binding via its PX domain to membrane curvature remodeling via its BAR domain. As a core component of heterodimeric SNX-BAR complexes of the Snx4 family (Snx4-Snx41, alternative to Snx4-Atg20/Snx42), it mediates retrograde transport from endosomes to the Golgi and promotes selective autophagy. In budding yeast, Snx41 can also form a complex with Atg24 competitively with Atg20; this Atg24-Atg20/Snx41 SNX-BAR complex localizes to the opening edge of the isolation membrane and keeps the phagophore mouth large enough for non-selective autophagic capture of large cytoplasmic assemblies (e.g. ribosomes, proteasomes). Within this complex Snx41 is partially redundant with Atg20 (snx41Ξ alone shows little autophagy defect). The protein localizes to endosomal compartments and the phagophore assembly site (PAS) through PI3P binding. While originally identified as a meiotically up-regulated gene (mug186), its upregulation during meiosis/sporulation reflects the increased autophagy that occurs during this developmental transition rather than a direct role in meiotic cell cycle regulation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000407 phagophore assembly site | IBA GO_REF:0000033 | ACCEPT | Summary: SNX41 localizes to the phagophore assembly site (PAS) during nitrogen starvation. The deep research extensively documents this localization, stating that SNX41 "localizes to endosomal compartments enriched in PI3P and the phagophore assembly site (PAS) in yeast cells" and that "SNX41 additionally localizes to punctate structures that associate with or are adjacent to autophagosomes." Reason: The IBA annotation is well-supported by experimental evidence showing PAS localization of SNX4 subfamily proteins during starvation. The PX domain mediates PI3P-dependent membrane targeting to PI3P-enriched pre-autophagosomal membranes. This represents a core aspect of SNX41 function in autophagy. Falcon deep research corroborates this via the Kotani et al. 2023 (budding yeast) finding that the Atg24-Atg20/Snx41 SNX-BAR complex localizes to the opening edge of the isolation membrane (phagophore) during autophagosome biogenesis. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md SNX41 functions as a core component of heterodimeric complexes, particularly within the SNX4 subfamily that includes Snx4/Atg24 and Atg20/Snx42, where it participates in both retromer-independent retrograde trafficking pathways and selective autophagy processes including pexophagy. The protein localizes to endosomal compartments enriched in PI3P and the phagophore assembly site (PAS) in yeast cells file:SCHPO/snx41/snx41-deep-research-perplexity.md SNX41 additionally localizes to punctate structures that associate with or are adjacent to autophagosomes, as determined by colocalization with the autophagy marker Atg8 (visualized as RFP-Atg8 in immunofluorescence studies) file:SCHPO/snx41/snx41-deep-research-falcon.md A major 2023 development is the discovery that a **sorting nexin complex localizes to the opening edge of the isolation membrane (IM)** (phagophore) and is critical for ensuring **non-selective sequestration** of cytoplasm during autophagosome biogenesis. |
| GO:0000422 autophagy of mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: SNX41 promotes mitophagy (autophagy of mitochondria) in fission yeast. The deep research states that "autophagy of ER and mitochondria is induced by nitrogen starvation and is promoted by three Atg20- and Atg24-family proteins" in S. pombe. While this directly refers to Atg20, Atg24, and Atg24b (SPBC1711.11), SNX41 belongs to this same protein family and has conserved autophagy functions. Reason: This annotation is supported by phylogenetic inference. SNX41 belongs to the SNX4 subfamily of sorting nexins that promote organelle autophagy. The deep research confirms that SNX41 "participates in selective autophagy pathways, particularly in the degradation of peroxisomes through a process termed pexophagy." The conservation of selective autophagy functions across SNX4 subfamily members supports mitophagy annotation. Falcon deep research adds important nuance: in budding yeast (Kotani et al. 2023) snx41Ξ alone shows little/no autophagy defect and is partially redundant with Atg20 within the Atg24 complex, so the contribution to organelle autophagy is real but family-redundant rather than uniquely Snx41-dependent. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md Beyond its well-characterized roles in retrograde trafficking, SNX41 participates in selective autophagy pathways, particularly in the degradation of peroxisomes through a process termed pexophagy (peroxisomal autophagy), where damaged or excess peroxisomes are selectively engulfed by autophagosomes and delivered to the vacuole for degradation file:SCHPO/snx41/snx41-deep-research-perplexity.md SNX41 functions within the broader context of cellular autophagy responses, participating in various selective autophagy pathways beyond pexophagy, including potential roles in the cytoplasm-to-vacuole targeting (Cvt) pathway and possibly mitophagy (selective autophagy of mitochondria) PMID:27737912 autophagy of ER and mitochondria is induced by nitrogen starvation and is promoted by three Atg20- and Atg24-family proteins - Atg20, Atg24 and SPBC1711.11 (named here as Atg24b) file:SCHPO/snx41/snx41-deep-research-falcon.md Kotani et al. report that **ATG24 knockout** and **double knockout of ATG20 and SNX41** βlargely promoted cell deathβ under nitrogen starvation, whereas **atg20Ξ** showed milder viability defects and **snx41Ξ** showed little/no defect, consistent with partial redundancy of Atg20 and Snx41 in the functional complex. |
| GO:0032266 phosphatidylinositol-3-phosphate binding | IBA GO_REF:0000033 | ACCEPT | Summary: SNX41 contains a PX domain that binds phosphatidylinositol-3-phosphate (PI3P). The deep research extensively documents this function, stating that the PX domain "serves as the primary determinant of membrane localization through its high-affinity binding to phosphatidylinositol 3-phosphate (PI3P)." UniProt annotates specific PI3P binding residues at positions 103, 105, 129, and 152. Reason: This molecular function annotation is well-supported by domain analysis and structural data. The PX domain is a defining feature of the sorting nexin family and is essential for PI3P-dependent membrane targeting. This is a core molecular function of SNX41. Falcon deep research corroborates the PX-PI3P/BAR architecture as the basis for membrane targeting and remodeling. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md The protein is defined by the presence of a canonical phox homology (PX) domain, a conserved ~100-130 amino acid motif that was first identified in the NADPH phagocyte oxidase complex and has subsequently been recognized as the defining feature of the entire sorting nexin protein family. This PX domain occupies a central position within the SNX41 sequence and serves as the primary determinant of membrane localization through its high-affinity binding to phosphatidylinositol 3-phosphate (PI3P) file:SCHPO/snx41/snx41-deep-research-perplexity.md The interaction between the PX domain and PI3P is not merely a simple lock-and-key recognition event but rather involves conformational changes in the protein structure that increase membrane affinity upon lipid binding, creating a cooperative binding mechanism file:SCHPO/snx41/snx41-deep-research-falcon.md Based on conserved SNX-BAR principles, Snx41βs **PX domain** supports recruitment to PI3P-enriched membranes, while the **BAR domain** supports dimeric scaffolding/curvature stabilizationβfunctions that are required to shape or stabilize membrane subdomains in trafficking and autophagy. |
| GO:0061709 reticulophagy | IBA GO_REF:0000033 | ACCEPT | Summary: SNX41 promotes reticulophagy (selective autophagy of endoplasmic reticulum) in fission yeast. The deep research indicates that Atg20- and Atg24-family proteins promote ER autophagy during nitrogen starvation. SNX41 belongs to this protein family with conserved autophagy functions. Reason: This annotation is supported by phylogenetic inference from the conserved autophagy functions of the SNX4 subfamily. The deep research documents extensive roles in selective autophagy pathways. This represents a core selective autophagy function based on family conservation. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md SNX41 functions within the broader context of cellular autophagy responses, participating in various selective autophagy pathways beyond pexophagy, including potential roles in the cytoplasm-to-vacuole targeting (Cvt) pathway and possibly mitophagy (selective autophagy of mitochondria) PMID:27737912 autophagy of ER and mitochondria is induced by nitrogen starvation and is promoted by three Atg20- and Atg24-family proteins |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: SNX41 is found in the cytoplasm based on UniProt subcellular location annotation. UniProt states "Cytoplasm" with evidence from PMID:16823372 (large-scale localization study in S. pombe). The deep research confirms this, noting that PX-deficient SNX41 "results in predominantly cytoplasmic distribution of the protein." Reason: This is a valid cellular component annotation. The protein localizes to cytoplasmic compartments including endosomes and perivacuolar structures. The IEA is consistent with more specific HDA evidence for cytosol localization. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md The localization of SNX41 to these membrane structures is largely dependent on the PX domain, as demonstrated by studies in which targeted deletion of the PX domain (generating SNX41delta215-627 lacking the N-terminal PX region) results in predominantly cytoplasmic distribution of the protein PMID:16823372 we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein |
| GO:0006914 autophagy | IEA GO_REF:0000043 | ACCEPT | Summary: SNX41 is involved in autophagy based on the UniProt keyword "Autophagy" (KW-0072). The deep research extensively documents SNX41's roles in selective autophagy, particularly pexophagy, and its integration with broader autophagy networks. Reason: This annotation is well-supported though somewhat general. SNX41 functions in selective autophagy pathways. The IEA is consistent with the more specific IBA annotations for mitophagy and reticulophagy. Acceptable as a broader classification. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md Through its essential roles in protein sorting, membrane remodeling, and autophagy regulation, SNX41 contributes to maintaining cellular homeostasis and represents an important node in the endocytic-autophagic axis that is conserved across eukaryotic organisms file:SCHPO/snx41/snx41-deep-research-perplexity.md SNX41 functions within the broader context of cellular autophagy responses, participating in various selective autophagy pathways beyond pexophagy |
| GO:0008289 lipid binding | IEA GO_REF:0000043 | ACCEPT | Summary: SNX41 binds lipids, specifically phosphatidylinositol-3-phosphate (PI3P), through its PX domain. This IEA is based on the UniProt keyword "Lipid-binding" (KW-0446). The deep research confirms extensive PI3P binding capacity. Reason: This is a valid but general molecular function annotation. SNX41 binds PI3P through its PX domain. More specific annotations for PI3P binding (GO:0032266) are available via IBA, but this broader term is not incorrect. Acceptable as a higher-level classification. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md This PX domain occupies a central position within the SNX41 sequence and serves as the primary determinant of membrane localization through its high-affinity binding to phosphatidylinositol 3-phosphate (PI3P), a phosphorylated lipid found enriched on endosomal and pre-autophagosomal membranes |
| GO:0010008 endosome membrane | IEA GO_REF:0000044 | ACCEPT | Summary: SNX41 localizes to endosome membranes as a peripheral membrane protein. UniProt states "Endosome membrane; Peripheral membrane protein" based on experimental evidence. The deep research extensively documents endosomal localization. Reason: This cellular component annotation is well-supported. SNX41 functions at endosomal membranes where it participates in retrograde transport. The localization is mediated by PI3P binding through the PX domain. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md The protein localizes to endosomal compartments enriched in PI3P and the phagophore assembly site (PAS) in yeast cells, enabling it to coordinate the retrieval of specific integral membrane proteins and lipids from the endosomal system and facilitate their recycling back to the trans-Golgi network file:SCHPO/snx41/snx41-deep-research-perplexity.md In wild-type fission yeast cells expressing SNX41-GFP fusion proteins under native regulation, the protein exhibits a punctate distribution pattern characteristic of endosomal localization, with individual foci representing distinct endosomal compartments or tubular carriers derived from endosomes |
| GO:0012505 endomembrane system | IEA GO_REF:0000044 | ACCEPT | Summary: SNX41 localizes to the endomembrane system. UniProt indicates "Endomembrane system; Peripheral membrane protein" based on subcellular location data. Reason: This is a valid but general cellular component annotation. SNX41 localizes to various endomembrane compartments including endosomes and the phagophore assembly site. More specific annotations are available but this broader term is acceptable. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md The protein localizes to endosomal compartments enriched in PI3P and the phagophore assembly site (PAS) in yeast cells PMID:16823372 we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome |
| GO:0015031 protein transport | IEA GO_REF:0000043 | ACCEPT | Summary: SNX41 is involved in protein transport, specifically retrograde transport from endosomes to the Golgi. This IEA is based on the UniProt keyword "Protein transport" (KW-0653). The deep research extensively documents cargo-specific sorting functions. Reason: This is a valid but general biological process annotation. SNX41 mediates retrograde transport of specific cargo proteins (e.g., Atg27, Snc1) from endosomes to the Golgi. More specific annotations for retrograde transport are available via ISO/IEA. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md A crucial functional role for SNX41 has been elucidated through its assembly into heterodimeric complexes with other SNX4 subfamily members, particularly through its interaction with Snx4/Atg24, where the two proteins form a Snx4-Snx41 heterodimer that functions as a distinct molecular entity with cargo-specific sorting capacity file:SCHPO/snx41/snx41-deep-research-perplexity.md The primary identified cargo of the Snx4-Snx41 pathway is Atg27, an integral membrane protein implicated in selective autophagy that cycles between the Golgi apparatus, endosomes, and autophagy-related compartments |
| GO:0035091 phosphatidylinositol binding | IEA GO_REF:0000002 | ACCEPT | Summary: SNX41 binds phosphatidylinositol through its PX domain. This IEA is based on InterPro domain annotations (IPR001683, IPR036871, IPR044106). Reason: This is a valid molecular function annotation. SNX41 specifically binds PI3P, which is a type of phosphatidylinositol. More specific annotations for PI3P binding (GO:0032266) are available via IBA, but this term is not incorrect as a parent term. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md The molecular basis for PI3P recognition by SNX41 resides in the specific structural arrangement of residues within the PX domain that form a binding pocket optimized for interaction with the phosphorylated inositol headgroup of the phosphatidylinositol lipid |
| GO:0042147 retrograde transport, endosome to Golgi | IEA GO_REF:0000002 | ACCEPT | Summary: SNX41 participates in retrograde transport from endosomes to the Golgi. This IEA is based on InterPro domain annotation (IPR044106 - PX_Snx41/Atg20). The deep research extensively documents this as a core function. Reason: This biological process annotation is core to SNX41 function. The Snx4-Snx41 heterodimer mediates retrograde transport of specific cargo proteins like Atg27 from post-Golgi endosomes back to the trans-Golgi network. Falcon deep research places Snx41-family proteins at the intersection of endosomal retrograde trafficking and autophagy/protein homeostasis. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md Live cell imaging studies combined with biochemical analyses have revealed that this Snx4-Snx41 heterodimer coats endosome-derived tubular carriers and mediates retrograde transport of specific cargo proteins from post-Golgi endosomes back to the trans-Golgi network (TGN) file:SCHPO/snx41/snx41-deep-research-perplexity.md The sorting nexin SNX41, along with Snx4 and Snx42/Atg20, is specifically required for the retrieval of the exocytic v-SNARE protein Snc1p from post-Golgi endosomes, with genetic and biochemical studies demonstrating that deletion of snx41 results in mislocalization of Snc1 to the vacuole file:SCHPO/snx41/snx41-deep-research-falcon.md Expert synthesis places Snx41-family proteins at the intersection of **endosomal retrograde trafficking** and **autophagy/protein homeostasis**, explaining why direct biochemical data for fission-yeast Snx41 remain limited but family-based functional inference is strong |
| GO:0051321 meiotic cell cycle | IEA GO_REF:0000043 | REMOVE | Summary: This IEA is based on the UniProt keyword "Meiosis" (KW-0469), which was assigned because SNX41 was originally identified as mug186 (meiotically up-regulated gene 186). However, the deep research is clear that this reflects increased autophagy demands during sporulation, not a direct role in meiotic cell cycle regulation. The research states that "SNX41 has specialized roles in fungal developmental programs" related to "membrane trafficking and reorganization" during sporulation. Reason: This annotation represents an over-annotation based on gene expression rather than function. The deep research clarifies that "The snx41 gene was originally identified in S. pombe as mug186 (meiotically up-regulated gene 186), indicating elevated expression during meiosis and sporulation." However, this upregulation supports autophagy during sporulation: "The remodeling of membrane systems during sporulation likely depends critically on retrograde trafficking pathways mediated by SNX41." The paper that identified mug186 (PMID:16303567) found that snx41/mug186 was NOT among the seven genes "required for critical meiotic events." SNX41 is a sorting nexin involved in autophagy and retrograde transport, with autophagy naturally upregulated during meiosis/sporulation. This describes increased demand for SNX41's core trafficking/autophagy functions, not a direct role in meiotic cell cycle control. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md The snx41 gene was originally identified in S. pombe as mug186 (meiotically up-regulated gene 186), indicating elevated expression during meiosis and sporulation, which directly implicates SNX41 in the developmental program controlling spore formation file:SCHPO/snx41/snx41-deep-research-perplexity.md The remodeling of membrane systems during sporulation likely depends critically on retrograde trafficking pathways mediated by SNX41, as these pathways ensure that membrane proteins required for spore development are properly localized and maintained in appropriate cellular compartments file:SCHPO/snx41/snx41-deep-research-perplexity.md The upregulation of SNX41 during meiosis suggests that SNX41-dependent trafficking becomes especially important during the developmental switch from mitotic growth to meiotic development, potentially to recycle proteins involved in mitotic cell cycle control and to promote new pathways required for sexual differentiation PMID:16303567 we have deleted 175 meiotically upregulated genes and found seven genes not previously reported to be critical for meiotic events |
| GO:0005515 protein binding | IPI PMID:27737912 Atg20- and Atg24-family proteins promote organelle autophagy... | MODIFY | Summary: SNX41 was shown to physically interact with other proteins. The GOA data indicates interaction with PomBase:SPAC6F6.12. The deep research documents that SNX41 functions primarily as a component of heterodimeric complexes with SNX4 subfamily members. Reason: The term "protein binding" (GO:0005515) is too general and uninformative. SNX41 forms specific heterodimeric complexes with Snx4/Atg24 family members. The deep research states "SNX41 functions primarily as a component of heterodimeric complexes rather than as a solitary protein" and describes "Snx4-Snx41 heterodimer" formation. A more informative annotation would describe protein dimerization activity. Falcon deep research independently confirms this complex behavior, noting that Snx41 can form a complex with Atg24 competitively with Atg20, and that Snx4 forms alternative heterodimers (Snx4-Snx41 or Snx4-Atg20/Snx42). Proposed replacements: protein dimerization activity Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md SNX41 functions primarily as a component of heterodimeric complexes rather than as a solitary protein, with the yeast SNX4 protein representing the primary obligate binding partner that enables SNX41 endosomal localization and autophagy-related functions file:SCHPO/snx41/snx41-deep-research-perplexity.md The Snx4-Snx41 heterodimer forms through interactions between the BAR domains of the two proteins, which dimerize to create the characteristic crescent-shaped architecture that enables membrane curvature sensing and induction PMID:27737912 S. pombe Atg24 forms a homo-oligomer and acts redundantly with Atg20 and Atg24b, and the latter two proteins can form a hetero-oligomer file:SCHPO/snx41/snx41-deep-research-falcon.md In yeast systems, Snx41 is described as part of a **Snx4-family** group (Snx4, Snx41, and Atg20/Snx42), where **Snx4 forms alternative heterodimers** (e.g., Snx4βSnx41 or Snx4βAtg20/Snx42) associated with distinct trafficking/autophagy roles. |
| GO:0005829 cytosol | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: SNX41 localizes to the cytosol based on high-throughput direct assay (HDA) from a large-scale protein localization study in S. pombe (PMID:16823372). This study used YFP-tagging to determine localization of approximately 90% of the fission yeast proteome. Reason: This annotation is supported by experimental evidence from a systematic localization study. SNX41 is found in the cytosol as well as associated with endosomal membranes. The HDA evidence from a large-scale study provides good support for this localization. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md The localization of SNX41 to these membrane structures is largely dependent on the PX domain, as demonstrated by studies in which targeted deletion of the PX domain (generating SNX41delta215-627 lacking the N-terminal PX region) results in predominantly cytoplasmic distribution of the protein PMID:16823372 we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein |
| GO:0005768 endosome | ISO GO_REF:0000024 | ACCEPT | Summary: SNX41 localizes to endosomes based on sequence orthology (ISO) with S. cerevisiae Snx41 (SGD:S000002833). UniProt indicates "Endosome and other perivacuolar punctate structures" for localization. The deep research extensively documents endosomal localization. Reason: This cellular component annotation is well-supported. SNX41 functions at endosomal compartments where it mediates retrograde transport. The ISO evidence from budding yeast ortholog is appropriate given the conserved function of SNX41 family proteins. Falcon deep research confirms SNX-BAR proteins are endosome-associated punctate structures. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md In wild-type fission yeast cells expressing SNX41-GFP fusion proteins under native regulation, the protein exhibits a punctate distribution pattern characteristic of endosomal localization, with individual foci representing distinct endosomal compartments or tubular carriers derived from endosomes file:SCHPO/snx41/snx41-deep-research-perplexity.md The subcellular localization of SNX41 is primarily determined by its PI3P-binding PX domain, which directs the protein to endosomal and autophagy-related membrane compartments where this phosphoinositide accumulates file:SCHPO/snx41/snx41-deep-research-falcon.md At the family level, SNX-BAR proteins are endosome-associated due to PI-binding and are often seen as punctate cytosolic/endosomal structures |
| GO:0042147 retrograde transport, endosome to Golgi | ISO GO_REF:0000024 | ACCEPT | Summary: SNX41 is involved in retrograde transport from endosomes to Golgi based on sequence orthology (ISO) with S. cerevisiae Snx41 (SGD:S000002833). This is a core function extensively documented in the deep research. Reason: This biological process annotation is core to SNX41 function and is well-supported by orthology to budding yeast Snx41 as well as extensive functional studies. Duplicate of IEA annotation but with different evidence source - both are valid. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md Live cell imaging studies combined with biochemical analyses have revealed that this Snx4-Snx41 heterodimer coats endosome-derived tubular carriers and mediates retrograde transport of specific cargo proteins from post-Golgi endosomes back to the trans-Golgi network (TGN) file:SCHPO/snx41/snx41-deep-research-perplexity.md In addition to its role in the Snx4-Snx41 complex, SNX41 participates in other retrograde sorting mechanisms that mediate the retrieval of specific membrane proteins from post-Golgi endosomes back to the Golgi apparatus |
| GO:0035091 phosphatidylinositol binding | ISM GO_REF:0000050 | ACCEPT | Summary: SNX41 binds phosphatidylinositol based on sequence model (ISM) matching the PX domain (Pfam:PF00787). Reason: This molecular function annotation is well-supported by domain architecture. The PX domain is a well-characterized phosphoinositide-binding domain. More specific PI3P binding annotation available via IBA. Duplicate of IEA annotation but with different evidence source - both are valid. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md The molecular basis for PI3P recognition by SNX41 resides in the specific structural arrangement of residues within the PX domain that form a binding pocket optimized for interaction with the phosphorylated inositol headgroup of the phosphatidylinositol lipid |
| GO:0000425 pexophagy | IBA GO_REF:0000033 | NEW | Summary: SNX41 is implicated in pexophagy (selective autophagy of peroxisomes) based on phylogenetic inference and extensive studies in related fungi. The deep research states that "SNX41 participates in selective autophagy pathways, particularly in the degradation of peroxisomes through a process termed pexophagy (peroxisomal autophagy)." Reason: Pexophagy is a well-documented function of SNX41 orthologs. The deep research extensively documents pexophagy function: "The involvement of SNX41 in pexophagy has been demonstrated through studies in both budding yeast and the rice blast fungus Magnaporthe oryzae, where SNX41-deletion mutants show defective pexophagy." UniProt also notes "May be required for cytoplasm to vacuole transport (Cvt) and pexophagy." This is a core selective autophagy function that should be annotated. Supporting Evidence: file:SCHPO/snx41/snx41-deep-research-perplexity.md Beyond its well-characterized roles in retrograde trafficking, SNX41 participates in selective autophagy pathways, particularly in the degradation of peroxisomes through a process termed pexophagy (peroxisomal autophagy), where damaged or excess peroxisomes are selectively engulfed by autophagosomes and delivered to the vacuole for degradation file:SCHPO/snx41/snx41-deep-research-perplexity.md The involvement of SNX41 in pexophagy has been demonstrated through studies in both budding yeast and the rice blast fungus Magnaporthe oryzae, where SNX41-deletion mutants show defective pexophagy as evidenced by accumulation of intact peroxisomes within cells that normally undergo efficient autophagy under nutrient starvation conditions file:SCHPO/snx41/snx41-uniprot.txt May be required for cytoplasm to vacuole transport (Cvt) and pexophagy |
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Download this section (compressed HTML)Q: What are the specific cargo proteins sorted by Snx4-Snx41 complexes in S. pombe, and how do they compare to budding yeast Snx4-Snx41 cargo such as Atg27?
Q: Does S. pombe snx41 have distinct pexophagy functions, or is pexophagy primarily mediated by other Atg20/Atg24 family members in fission yeast?
Experiment: Pexophagy assays in S. pombe snx41 mutants to confirm pexophagy function. This would provide direct evidence for pexophagy function in fission yeast, currently inferred from other fungi and phylogenetic conservation.
Experiment: Cargo identification studies using Snx4-Snx41 affinity purification in S. pombe to identify the specific retrograde transport cargo in fission yeast.
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