Affinage · Toxoplasma gondii

CDC48AP

cell division protein CDC48AP · UniProt A0A125YJG8

Annotated
2026-09-08
1 papers in source corpus 1 papers cited in narrative 2 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CDC48AP is an AAA ATPase motor that drives translocation of nucleus-encoded apicoplast proteins across the periplastid membrane during apicoplast protein import in Toxoplasma gondii (PMID:28655825). It operates within an apicoplast-specific ERAD-like complex together with the plastid ubiquitin-like protein (PUBL), coupling ubiquitin-like conjugation to the membrane translocation step (PMID:28655825). Conditional null mutants establish that CDC48AP is essential both for this translocation and for parasite survival (PMID:28655825). Beyond its role as the translocation motor in the CDC48AP–PUBL ERAD-like complex, no further mechanistic detail has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2017 High

    It was unknown how nucleus-encoded proteins cross the periplastid membrane into the apicoplast; conditional deletion identified CDC48AP as an essential AAA ATPase driving this translocation step.

    Evidence Conditional null mutants with genetic complementation and functional import assays in Toxoplasma gondii

    PMID:28655825

    Open questions at the time
    • ATPase catalytic mechanism and nucleotide-cycle coupling to translocation not resolved
    • Full set of translocated substrates not defined
    • Structural organization of the motor at the periplastid membrane unknown
  2. 2017 High

    The question of how translocation is coupled to a ubiquitin-like signal was addressed by showing CDC48AP acts with PUBL in an apicoplast-specific ERAD-like complex at the periplastid membrane.

    Evidence Genetic interaction/epistasis via conditional null mutants of both CDC48AP and PUBL with functional complementation in Toxoplasma gondii

    PMID:28655825

    Open questions at the time
    • Physical composition of the ERAD-like complex and additional subunits not defined
    • Nature of the ubiquitin-like conjugation events coupled to translocation not detailed
    • Direct biochemical interaction between CDC48AP and PUBL not shown

Open questions

Synthesis pass · forward-looking unresolved questions
  • The biochemical and structural basis of how CDC48AP recognizes, engages, and unfolds substrates and mechanistically links PUBL conjugation to ATP-driven translocation remains unresolved.
  • No structural model of the CDC48AP motor or ERAD-like complex
  • No enumerated substrate repertoire
  • Mechanism of substrate recognition and unfolding uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Partners
PUBL (PLASTID UBIQUITIN-LIKE PROTEIN)
Complex memberships
Apicoplast-specific ERAD-like complex (CDC48AP–PUBL) at the periplastid membrane

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2017 CDC48AP, an AAA ATPase, functions to translocate apicoplast proteins across the periplastid membrane during protein import into the apicoplast. Conditional null mutants demonstrate CDC48AP is essential for this translocation process and for parasite survival. Conditional null mutants, genetic complementation, functional import assays mBio High 28655825
2017 CDC48AP acts together with the plastid ubiquitin-like protein (PUBL) as part of an apicoplast-specific ERAD-like complex at the periplastid membrane, coupling ubiquitin-like conjugation to protein translocation across this membrane during apicoplast protein import. Genetic interaction / epistasis via conditional null mutants of both CDC48AP and PUBL, functional complementation mBio High 28655825

Source papers

Stage 0 corpus · 1 paper · ranked by NIH iCite citations
Year Title Journal Citations PMID
2017 A Plastid Protein That Evolved from Ubiquitin and Is Required for Apicoplast Protein Import in Toxoplasma gondii. mBio 28 28655825