April 17, 1998FEBS Letters

The GXGXG motif in the pICln protein is not important for the nucleotide sensitivity of the pICln‐induced Cl− current in Xenopus oocytes

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Population

Xenopus laevis oocytes injected with RNA encoding a rat mutant pI in which the three glycines of the…

Design

Preclinical

Authors

TVThomas VoetsVIB-KU Leuven Center for Microbiology GBGunnar BuyseKU Leuven GDGuy DroogmansUniversity of Debrecen

Discussion

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Implication

Challenges hypothesis that GXGXG motif is pICln extracellular nucleotide-binding site; hypothesis-generating for alternative mechanisms.

Structured PICO

Population

Xenopus laevis oocytes injected with RNA encoding a rat mutant pI(Cln) in which the three glycines of the putative nucleotide-binding site have been changed into alanines (G54A; G56A; G58A)

Intervention

Mutation of the GXGXG motif (three glycines changed to alanines)

Outcome

Nucleotide sensitivity of the pICln-induced Cl- current (voltage-dependent block by extracellular cAMP)surrogate

The GXGXG motif in the pICln protein is not essential for the nucleotide sensitivity of the pICln-induced Cl- current, challenging the hypothesis of it being an extracellular nucleotide-binding site.

Cite This Study

Voets et al. (1998) studied this question.

synapsesocial.com/papers/6a96ed3c65cd0d1d26bb7d8b https://doi.org/10.1016/s0014-5793(98)00334-2

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The GXGXG motif in the pICln protein is not important for the nucleotide sensitivity of the pICln‐induced Cl− current in Xenopus oocytes

Discussion

Member takes

Implication

Structured PICO

Cite This Study

The GXGXG motif in the pICln protein is not important for the nucleotide sensitivity of the pICln‐induced Cl− current in Xenopus oocytes

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider