PHLP2 is essential and plays a role in ciliogenesis and microtubule assembly in Tetrahymena thermophila
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Summary
In Tetrahymena, PhLP2 is essential and under specific experimental conditions its activity affects tubulin and microtubule‐dependent functions including cilia assembly, which is investigated by deleting its single homolog, Phlp2p.
- Type
- article
- Published
- 2013-11-01
- Cited by
- 18
- References
- 84
- OpenAlex
- https://openalex.org/W23588994
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:19289345
Keywords
Chemistry, Chemisorption, Coulometry, Inorganic chemistry, Platinum
References
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Cited by
- Essential role of the chaperonin CCT in rod outer segment biogenesis.
- Arginine deprivation affects glioblastoma cell adhesion, invasiveness and actin cytoskeleton organization by impairment of β-actin arginylation
- Primary cilia and kidney injury: current research status and future perspectives.
- Interaction of a Novel Chaperone PhLP2A With the Heat Shock Protein Hsp90
- Regulation of katanin activity in the ciliate Tetrahymena thermophila
- Ciliary proteins Fap43 and Fap44 interact with each other and are essential for proper cilia and flagella beating
- Multiple phosphorylation sites on γ‐tubulin are essential and contribute to the biogenesis of basal bodies in Tetrahymena
- Motile Cilia: Innovation and Insight From Ciliate Model Organisms
- The LisH Domain-Containing N-Terminal Fragment is Important for the Localization, Dimerization, and Stability of Katnal2 in Tetrahymena
- Ccdc113/Ccdc96 complex, a novel regulator of ciliary beating that connects radial spoke 3 to dynein g and the nexin link
- Composition and function of the C1b/C1f region in the ciliary central apparatus
- Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT
- Advancing ASMS with LC-MS/MS for the discovery of novel PDCL2 ligands from DNA-encoded chemical library selections
- PDCL2 is essential for spermiogenesis and male fertility in mice
- Cfap91-Dependent Stability of the RS2 and RS3 Base Proteins and Adjacent Inner Dynein Arms in Tetrahymena Cilia
- An amino acid-resolution interactome for motile cilia illuminates the structure and function of ciliopathy protein complexes
- An amino acid-resolution interactome for motile cilia identifies the structure and function of ciliopathy protein complexes
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