spo2

UniProt ID: C6Y4C2
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Review Status: COMPLETE
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Gene Description

Spo2 is a meiosis-induced spindle pole body protein that connects Spo15 with Spo13 on the cytoplasmic face of the meiotic spindle pole body. Its ordered recruitment is required for remodeling the spindle pole body and initiating forespore membrane formation during sporulation. It is not required for the meiotic nuclear divisions themselves.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0005515 protein binding
IPI
PMID:18367542
Meiotic spindle pole bodies acquire the ability to assemble ...
MODIFY
Summary: Spo2 bridges the Spo15 and Spo13 components of the meiotic spindle pole body.
Reason: Physical association with both partners, absence of direct Spo13–Spo15 interaction, and the Spo2 dependence of Spo13 recruitment support an adaptor mechanism more informative than generic protein binding. The replacement describes the integrated mechanism; neither interaction alone establishes it.
Proposed replacements: molecular adaptor activity
Supporting Evidence:
PMID:18367542
Spo2 physically associated with both Spo15 and Spo13, but Spo13 and Spo15 did not interact directly.
GO:0005515 protein binding
IPI
PMID:18367542
Meiotic spindle pole bodies acquire the ability to assemble ...
MODIFY
Summary: Spo2 bridges the Spo15 and Spo13 components of the meiotic spindle pole body.
Reason: Physical association with both partners, absence of direct Spo13–Spo15 interaction, and the Spo2 dependence of Spo13 recruitment support an adaptor mechanism more informative than generic protein binding. The replacement describes the integrated mechanism; neither interaction alone establishes it.
Proposed replacements: molecular adaptor activity
Supporting Evidence:
PMID:18367542
Spo2 physically associated with both Spo15 and Spo13, but Spo13 and Spo15 did not interact directly.
GO:0005816 spindle pole body
IEA
GO_REF:0000044
MODIFY
Summary: Spo2 specifically associates with the meiotic spindle pole body.
Reason: The localization is restricted to the sporulation-associated SPB rather than constitutive SPB residence.
Proposed replacements: meiotic spindle pole body
Supporting Evidence:
PMID:18367542
Spo13 and Spo2 localized on the cytoplasmic side of the SPB in close contact with the nascent FSM.
GO:0030437 ascospore formation
IMP
PMID:18367542
Meiotic spindle pole bodies acquire the ability to assemble ...
ACCEPT
Summary: Spo2 is required for ascospore formation.
Reason: Deletion blocks SPB modification and initiation of the forespore membrane while permitting meiotic nuclear division; sporulation is the principal biological role.
Supporting Evidence:
PMID:18367542
The respective deletion mutants are viable, but defective in SPB modification and in the onset of FSM formation.
GO:0031322 ascospore-type prospore-specific spindle pole body remodeling
IMP
PMID:18367542
Meiotic spindle pole bodies acquire the ability to assemble ...
ACCEPT
Summary: Spo2 enables sporulation-specific spindle pole body remodeling.
Reason: The target-gene mutant and ordered recruitment experiments directly establish this step in forespore membrane assembly.
Supporting Evidence:
PMID:18367542
The respective deletion mutants are viable, but defective in SPB modification and in the onset of FSM formation.
PMID:18367542
Spo2 physically associated with both Spo15 and Spo13, but Spo13 and Spo15 did not interact directly.
GO:0035974 meiotic spindle pole body
IDA
PMID:18367542
Meiotic spindle pole bodies acquire the ability to assemble ...
ACCEPT
Summary: Spo2 localizes to the cytoplasmic face of the meiotic spindle pole body.
Reason: Target-specific imaging and recruitment experiments support the meiotic SPB location; proximity to nascent membrane does not by itself establish membrane insertion.
Supporting Evidence:
PMID:18367542
Spo13 and Spo2 localized on the cytoplasmic side of the SPB in close contact with the nascent FSM.

Core Functions

Bridges Spo15 and Spo13 at the meiotic spindle pole body to initiate forespore membrane assembly.

Supporting Evidence:
  • PMID:18367542
    Spo2 physically associated with both Spo15 and Spo13, but Spo13 and Spo15 did not interact directly.
  • PMID:18367542
    The respective deletion mutants are viable, but defective in SPB modification and in the onset of FSM formation.

References

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Deep Research

Falcon

(spo2-deep-research-falcon.md)

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πŸ“š Additional Documentation

Notes

(spo2-notes.md)

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