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Glycobiology Advance Access published online on February 9, 2005
Glycobiology, doi:10.1093/glycob/cwi048
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org
Received August 29, 2004
Revised January 8, 2005
Accepted February 2, 2005

Article

Characterization of inhibitory signaling motifs of the natural killer cell receptor Siglec-7: Attenuated recruitment of phosphatases by the receptor is attributed to two amino acids in the motifs

Toshiyuki Yamaji 1, Motoaki Mitsuki1 2, Takane Teranishi 2, and Yasuhiro Hashimoto 3*

1 Glyco-chain Functions Laboratory, Supra-biomolecular System Group, Frontier Research System, Institute of Physical and Chemical Research (RIKEN), Wako-shi, Saitama 351-0198; Department of Anatomy, University of California San Francisco, 600 16th Street, San Francisco, CA 94143
2 Glyco-chain Functions Laboratory, Supra-biomolecular System Group, Frontier Research System, Institute of Physical and Chemical Research (RIKEN), Wako-shi, Saitama 351-0198;
3 Glyco-chain Functions Laboratory, Supra-biomolecular System Group, Frontier Research System, Institute of Physical and Chemical Research (RIKEN), Wako-shi, Saitama 351-0198; CREST, Japan Science and Technology Agency, Kawaguchi, Saitama 560-0082, Japan

* To whom correspondence should be addressed.
Yasuhiro Hashimoto, E-mail: yasua{at}postman.riken.go.jp


  Abstract

Siglec-7 (p75/AIRM1) is an inhibitory receptor on human natural killer cells and monocytes. The cytoplasmic domain of Siglec-7 contains two signaling motifs: a membrane-proximal immunoreceptor tyrosine-based inhibitory motif (Ile435-Gln-Tyr-Ala-Pro-Leu440) and a membrane-distal motif (Asn458-Glu-Tyr-Ser-Glu-Ile463). We report here that, upon pervanadate treatment, Siglec-7 recruited the protein tyrosine phosphatases SHP-1 and -2 less efficiently than did other inhibitory receptors such as Siglec-9 and leukocyte-associated Iglike receptor-1. Alignment of the amino acid sequences of the two Siglecs revealed only three amino acids difference in these motifs. To identify the amino acid(s) critical to recruitment efficiency, we prepared a series of Siglec-7-based mutants in which each of the three amino acids were replaced with the corresponding one of Siglec-9 (I435L, P439S, and N458T mutants). P439S and N458T mutants showed pronounced enhancement of SHP recruitment, but I435L mutant did a little effect. A double mutant (P439S, N458T) or triple mutant (I435L, P439S, N458T) recruited SHPs as much as did Siglec-9, indicating that Pro439 in the proximal motif and Asn458 in the distal motif of Siglec-7 attenuate its ability to recruit phosphatases. These amino acids appeared to affect not only phosphatase recruitment but also the subsequent attenuation of Syk phosphorylation.

Keywords: inhibitory motif/mutational analysis/Siglec/tyrosine phosphatase.
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