High impact information on Kcnip1

• Differential modulation of Kv4 kinetics by KCHIP1 splice variants [1].
• Remodelling inactivation gating of Kv4 channels by KChIP1, a small-molecular-weight calcium-binding protein [2].
• To investigate their mechanism of action, Kv4.1 or Kv4.3 were expressed in Xenopus laevis oocytes, either alone or together with KChIP1, and the K+ currents were recorded using the whole-oocyte voltage-clamp and patch-clamp methods [2].
• Qualitative PCR identified transcripts encoding the four known members of the KChIP family in isolated colonic and jejunal myocytes [3].
• Thus, changes in unitary conductance do not contribute to current upregulation by KChIP1 [2].

Biological context of Kcnip1

• Unanticipated Region- and Cell-Specific Downregulation of Individual KChIP Auxiliary Subunit Isotypes in Kv4.2 Knock-Out Mouse Brain [4].
• Structure, alternative splicing, and expression of the human and mouse KCNIP gene family [5].

Anatomical context of Kcnip1

• KChIP1 was expressed in a subpopulation of neurons widely distributed in brain and enriched in Purkinje cells of the cerebellum and in the reticular thalamic and medial habenular nuclei [6].
• From this we conclude that Kv4.3, in association with KChIP1, is the major molecular determinant of I(A) in murine colonic myocytes [3].
• However, the relative abundance of KChIP transcript was 2.6-fold greater in colon tissue than in jejunum, as assessed by quantitative PCR, with KChIP1 showing predominance [3].

Other interactions of Kcnip1

• The impact of Kv4.2 deletion on KChIP expression also supports the major role of KChIPs as auxiliary subunits of Kv4 channels [4].
• For example, KChIP1, KChIP2, and CALP can all bind presenilins and can all modulate A-type potassium channels [7].

References