Publication Date:
2003-08-02
Description:
Axonal voltage-gated potassium (Kv1) channels regulate action-potential invasion and hence transmitter release. Although evolutionarily conserved, what mediates their axonal targeting is not known. We found that Kv1 axonal targeting required its T1 tetramerization domain. When fused to unpolarized CD4 or dendritic transferrin receptor, T1 promoted their axonal surface expression. Moreover, T1 mutations eliminating Kvbeta association compromised axonal targeting, but not surface expression, of CD4-T1 fusion proteins. Thus, proper association of Kvbeta with the Kv1 T1 domain is essential for axonal targeting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Chen -- Jan, Yuh Nung -- Jan, Lily Yeh -- New York, N.Y. -- Science. 2003 Aug 1;301(5633):646-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Departments of Physiology and Biochemistry, University of California, San Francisco, CA 94143-0725, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12893943" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Motifs
;
Amino Acid Substitution
;
Animals
;
Antigens, CD4/metabolism
;
Axons/*metabolism
;
Biopolymers
;
COS Cells
;
Cell Line
;
Cell Membrane/metabolism
;
Cell Polarity
;
Cells, Cultured
;
Dendrites/metabolism
;
Endocytosis
;
Hippocampus/cytology
;
Humans
;
Kv1.2 Potassium Channel
;
Models, Molecular
;
Mutagenesis
;
Neurons/metabolism
;
Potassium Channels/*chemistry/*metabolism
;
*Potassium Channels, Voltage-Gated
;
*Protein Structure, Tertiary
;
Receptors, Transferrin/metabolism
;
Recombinant Fusion Proteins/chemistry/metabolism
;
Shaker Superfamily of Potassium Channels
;
Shal Potassium Channels
;
Transfection
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
