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J. Biol. Chem., Vol. 277, Issue 17, 14965-14975, April 26, 2002
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From the Presenilin (PS) genes linked to early-onset
familial Alzheimer's disease encode polytopic membrane proteins that
are presumed to constitute the catalytic subunit of The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF302044, AF305072, and AAG36976.
Molecular Cloning and Characterization of CALP/KChIP4, a Novel
EF-hand Protein Interacting with Presenilin 2 and Voltage-gated
Potassium Channel Subunit Kv4*
,,,,, and¶
Department of Neuropathology and
Neuroscience, Graduate School of Pharmaceutical Sciences, University of
Tokyo, Tokyo 113-0033 and § Department of Molecular and
Cellular Pharmacology, Graduate School of Pharmaceutical Sciences,
Nagoya City University, 467-8603 Nagoya, Japan
-secretase,
forming a high molecular weight complex with other proteins. During our attempts to identify binding partners of PS2, we cloned CALP
(calsenilin-like protein)/KChIP4, a
novel member of calsenilin/KChIP protein family that interacts with the
C-terminal region of PS. Upon co-expression in cultured cells, CALP was
directly bound to and co-localized with PS2 in endoplasmic reticulum.
Overexpression of CALP did not affect the metabolism or stability of PS
complex, and -cleavage of 
APP or Notch site 3 cleavage was not
altered. However, co-expression of CALP and a voltage-gated potassium
channel subunit Kv4.2 reconstituted the features of A-type
K+ currents and CALP directly bound Kv4.2, indicating
that CALP functions as KChIPs that are known as components of native
Kv4 channel complex. Taken together, CALP/KChIP4 is a novel EF-hand protein interacting with PS as well as with Kv4 that may modulate functions of a subset of membrane proteins in brain.
*
This work was supported by grants-in-aid from the Ministry
of Health and Welfare, the Ministry of Education, Science, Culture and
Sports, and CREST of Japan Science and Technology Corp., Japan.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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