Abstract
The N-terminus of rabbit Kv1.3 contains a signal sequence which regulates expression of Kv1.3 proteins in the plasma membrane. Removal of an N-terminal region (aa3-39) produced an increase in expressed K+ current. Progressive deletion at the N-terminus demonstrated that the shortest deletion required for the elevation of K current is D6-34. Since the functional signal sequence must include both ends of the peptide segment aa6-34 where charged residues are densely distributed, it is conceivable that this N-terminal signal sequence is related to charge or its associated hydrophilicity. Removal of two charged residues (31R, 33E) through amino acid substitution which converts deletion construct D3-27 to D3-27* effectively raises the amplitude of expressed current, further indicating the importance of charged residues. With the use of a mutated dynamin and a soluble N-terminal peptide, we also revealed that the N-terminal signal sequence may not act through the endocytotic pathway.
Original language | English |
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Pages (from-to) | 492-498 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 249 |
Issue number | 2 |
DOIs | |
Publication status | Published - 19 Aug 1998 |
Scopus Subject Areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology