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KCNIP1  -  Kv channel interacting protein 1

Homo sapiens

Synonyms: A-type potassium channel modulatory protein 1, KCHIP1, KChIP1, Kv channel-interacting protein 1, Potassium channel-interacting protein 1, ...
 
 
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High impact information on KCNIP1

  • Here, using mutagenesis and X-ray crystallography, we explore the interaction between Kv4 subunits and KChIP1 [1].
  • Coexpression of KChIP1 resulted in traffic of the channel to the plasma membrane, and traffic was abolished when mutations were introduced into the EF-hands with channel captured on vesicular structures that colocalized with KChIP1(2-4)-EYFP [2].
  • The membrane localisation of each NCS protein required myristoylation and minimal myristoylation motifs of hippocalcin or KChIP1 were sufficient to target fusion proteins to either TGN/plasma membrane or to punctate structures [3].
  • Myristoylation and correct targeting of KChIP1 was required for the efficient traffic of ECFP-Kv4.2 to the plasma membrane [3].
  • Residues within the myristoylation motif determine intracellular targeting of the neuronal Ca2+ sensor protein KChIP1 to post-ER transport vesicles and traffic of Kv4 K+ channels [3].
 

Biological context of KCNIP1

  • Pull-down assay revealed that the intact EF-hands 3 and 4 of KChIP1 were critical for CTX3-binding [4].
  • Elucidating KChIP effects on Kv4.3 inactivation and recovery kinetics with a minimal KChIP2 isoform [5].
  • Human K(v) channel interacting protein 1 (KCHIP1) is a new member of the neural calcium binding protein superfamily [6].
 

Anatomical context of KCNIP1

  • The resulting simulations illustrate ways in which KChIP2- and Ca(2+)-dependent control of I(Kv43) can result in a sustained outward current that can neutralize I(NaL) in a rate- and myocyte subtype-dependent manner [7].
  • We have explored factors affecting the localisation of Kv4.2 and the targeting of KChIP1 and other NCS proteins by using GFP-variant fusion proteins expressed in HeLa cells [3].
  • Then, through the techniques of fused green fluorescence protein and site-directed mutagenesis, we demonstrated that wild type KCHIP1 protein accumulated in the secretory vesicles of Golgi body [6].
  • In the case of hippocalcin and NCS-1, or alternatively KChIP1 (K+ channel-interacting protein 1), their N-terminal myristoylation motifs are sufficient for targeting to distinct organelles [8].
 

Associations of KCNIP1 with chemical compounds

  • Likewise, removal of EF-hands 3 and 4 distorted the ability of KChIP1 to bind with Kv4.2 N-terminal fragment (KvN) as well as fluorescent probe 8-anilinonaphthalene-1-sulfonate (ANS) [4].
  • The potential ability of KChIP EF-hands to sense intracellular Ca(2+) levels and transduce these changes to alterations in Kv4 channel inactivation kinetics may serve as a mechanism allowing intracellular Ca(2+) transients to modulate repolarization [5].
  • Molecular modeling using the KChIP1 crystal structure indicates that compound binding may occur in a small tryptophan-containing binding pocket located on the hydrophilic side of the protein [9].
 

Analytical, diagnostic and therapeutic context of KCNIP1

  • Western blot analysis revealed immunoreactive bands specific for Kv4.3, Kv1.4, and Kv channel-interacting protein (KChIP)2 in dog and human, but with notable differences in band sizes across species [10].
  • CL-888 altered the apparent affinity of KChIP1 to Kv4.3-N in a Biacore assay, but did not dissociate the two proteins in size-exclusion chromatography experiments [9].
  • In this study, a yeast two-hybrid assay was used to identify inhibitors such as a diaryl-urea compound (CL-888) that binds to and modulates the formation of the Kv4/KChIP complex [9].

References

  1. Two N-terminal domains of Kv4 K(+) channels regulate binding to and modulation by KChIP1. Scannevin, R.H., Wang, K., Jow, F., Megules, J., Kopsco, D.C., Edris, W., Carroll, K.C., Lü, Q., Xu, W., Xu, Z., Katz, A.H., Olland, S., Lin, L., Taylor, M., Stahl, M., Malakian, K., Somers, W., Mosyak, L., Bowlby, M.R., Chanda, P., Rhodes, K.J. Neuron (2004) [Pubmed]
  2. Traffic of Kv4 K+ channels mediated by KChIP1 is via a novel post-ER vesicular pathway. Hasdemir, B., Fitzgerald, D.J., Prior, I.A., Tepikin, A.V., Burgoyne, R.D. J. Cell Biol. (2005) [Pubmed]
  3. Residues within the myristoylation motif determine intracellular targeting of the neuronal Ca2+ sensor protein KChIP1 to post-ER transport vesicles and traffic of Kv4 K+ channels. O'Callaghan, D.W., Hasdemir, B., Leighton, M., Burgoyne, R.D. J. Cell. Sci. (2003) [Pubmed]
  4. Evidence showing an intermolecular interaction between KChIP proteins and Taiwan cobra cardiotoxins. Lin, Y.L., Lin, S.R., Wu, T.T., Chang, L.S. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  5. Elucidating KChIP effects on Kv4.3 inactivation and recovery kinetics with a minimal KChIP2 isoform. Patel, S.P., Campbell, D.L., Strauss, H.C. J. Physiol. (Lond.) (2002) [Pubmed]
  6. Experimental study on the new significant function domains of KCHIP1 protein. Liu, Z., Xiao, X.J., Fan, F.Y., Sun, Y.M., Li, Y.M., Yang, F.J. Sheng li xue bao [Acta physiologica Sinica]. (2005) [Pubmed]
  7. Contributions of sustained INa and IKv43 to transmural heterogeneity of early repolarization and arrhythmogenesis in canine left ventricular myocytes. Flaim, S.N., Giles, W.R., McCulloch, A.D. Am. J. Physiol. Heart Circ. Physiol. (2006) [Pubmed]
  8. High-affinity interaction of the N-terminal myristoylation motif of the neuronal calcium sensor protein hippocalcin with phosphatidylinositol 4,5-bisphosphate. O'Callaghan, D.W., Haynes, L.P., Burgoyne, R.D. Biochem. J. (2005) [Pubmed]
  9. Identification and characterization of small molecule modulators of KChIP/Kv4 function. Bowlby, M.R., Chanda, P., Edris, W., Hinson, J., Jow, F., Katz, A.H., Kennedy, J., Krishnamurthy, G., Pitts, K., Ryan, K., Zhang, H., Greenblatt, L. Bioorg. Med. Chem. (2005) [Pubmed]
  10. Phenotypic differences in transient outward K+ current of human and canine ventricular myocytes: insights into molecular composition of ventricular Ito. Akar, F.G., Wu, R.C., Deschenes, I., Armoundas, A.A., Piacentino, V., Houser, S.R., Tomaselli, G.F. Am. J. Physiol. Heart Circ. Physiol. (2004) [Pubmed]
 
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