LOK is a novel mouse STE20-like protein kinase that is expressed predominantly in lymphocytes

Satomi Kuramochi, Tetsuo Moriguchi, Keisuke Kuida, Junji Endo, Kentaro Senba, Eisuke Nishida, Hajime Karasuyama

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

We have identified a new gene, designated lok (lymphocyte-oriented kinase), that encodes a 966-amino acid protein kinase whose catalytic domain at the N terminus shows homology to that of the STE20 family members involved in mitogen-activated protein (MAP) kinase cascades. The non-catalytic domain of LOK does not have any similarity to that of other known members of the family. There is a proline-rich motif with Src homology region 3 binding potential, followed by a long coiled-coil structure at the C terminus. LOK is expressed as a 130-kDa protein, which was detected predominantly in lymphoid organs such as spleen, thymus, and bone marrow, in contrast to other mammalian members of the STE20 family. LOK phosphorylated itself as well as substrates such as myelin basic protein and histone IIA on serine and threonine residues but not on tyrosine residues, establishing LOK as a novel serine/threonine kinase. When coexpressed in COS7 cells with the known MAP kinase isoforms (ERK, JNK, and p38), LOK activated none of them in contrast to PAK- and GCK-related kinases. These results suggest that LOK could be involved in a novel signaling pathway in lymphocytes, which is distinct from the known MAP kinase cascades.

Original languageEnglish
Pages (from-to)22679-22684
Number of pages6
JournalJournal of Biological Chemistry
Volume272
Issue number36
DOIs
Publication statusPublished - 1997 Sep 5
Externally publishedYes

Fingerprint

Lymphocytes
Mitogen-Activated Protein Kinases
Protein Kinases
Phosphotransferases
Thymus
Myelin Basic Protein
Protein-Serine-Threonine Kinases
Threonine
Proline
Histones
Serine
Thymus Gland
Tyrosine
Catalytic Domain
Protein Isoforms
Bone
Spleen
Genes
Bone Marrow
Amino Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

LOK is a novel mouse STE20-like protein kinase that is expressed predominantly in lymphocytes. / Kuramochi, Satomi; Moriguchi, Tetsuo; Kuida, Keisuke; Endo, Junji; Senba, Kentaro; Nishida, Eisuke; Karasuyama, Hajime.

In: Journal of Biological Chemistry, Vol. 272, No. 36, 05.09.1997, p. 22679-22684.

Research output: Contribution to journalArticle

Kuramochi, S, Moriguchi, T, Kuida, K, Endo, J, Senba, K, Nishida, E & Karasuyama, H 1997, 'LOK is a novel mouse STE20-like protein kinase that is expressed predominantly in lymphocytes', Journal of Biological Chemistry, vol. 272, no. 36, pp. 22679-22684. https://doi.org/10.1074/jbc.272.36.22679
Kuramochi, Satomi ; Moriguchi, Tetsuo ; Kuida, Keisuke ; Endo, Junji ; Senba, Kentaro ; Nishida, Eisuke ; Karasuyama, Hajime. / LOK is a novel mouse STE20-like protein kinase that is expressed predominantly in lymphocytes. In: Journal of Biological Chemistry. 1997 ; Vol. 272, No. 36. pp. 22679-22684.
@article{3b2c83093ff44cc48465a6bbdf0eb534,
title = "LOK is a novel mouse STE20-like protein kinase that is expressed predominantly in lymphocytes",
abstract = "We have identified a new gene, designated lok (lymphocyte-oriented kinase), that encodes a 966-amino acid protein kinase whose catalytic domain at the N terminus shows homology to that of the STE20 family members involved in mitogen-activated protein (MAP) kinase cascades. The non-catalytic domain of LOK does not have any similarity to that of other known members of the family. There is a proline-rich motif with Src homology region 3 binding potential, followed by a long coiled-coil structure at the C terminus. LOK is expressed as a 130-kDa protein, which was detected predominantly in lymphoid organs such as spleen, thymus, and bone marrow, in contrast to other mammalian members of the STE20 family. LOK phosphorylated itself as well as substrates such as myelin basic protein and histone IIA on serine and threonine residues but not on tyrosine residues, establishing LOK as a novel serine/threonine kinase. When coexpressed in COS7 cells with the known MAP kinase isoforms (ERK, JNK, and p38), LOK activated none of them in contrast to PAK- and GCK-related kinases. These results suggest that LOK could be involved in a novel signaling pathway in lymphocytes, which is distinct from the known MAP kinase cascades.",
author = "Satomi Kuramochi and Tetsuo Moriguchi and Keisuke Kuida and Junji Endo and Kentaro Senba and Eisuke Nishida and Hajime Karasuyama",
year = "1997",
month = "9",
day = "5",
doi = "10.1074/jbc.272.36.22679",
language = "English",
volume = "272",
pages = "22679--22684",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "36",

}

TY - JOUR

T1 - LOK is a novel mouse STE20-like protein kinase that is expressed predominantly in lymphocytes

AU - Kuramochi, Satomi

AU - Moriguchi, Tetsuo

AU - Kuida, Keisuke

AU - Endo, Junji

AU - Senba, Kentaro

AU - Nishida, Eisuke

AU - Karasuyama, Hajime

PY - 1997/9/5

Y1 - 1997/9/5

N2 - We have identified a new gene, designated lok (lymphocyte-oriented kinase), that encodes a 966-amino acid protein kinase whose catalytic domain at the N terminus shows homology to that of the STE20 family members involved in mitogen-activated protein (MAP) kinase cascades. The non-catalytic domain of LOK does not have any similarity to that of other known members of the family. There is a proline-rich motif with Src homology region 3 binding potential, followed by a long coiled-coil structure at the C terminus. LOK is expressed as a 130-kDa protein, which was detected predominantly in lymphoid organs such as spleen, thymus, and bone marrow, in contrast to other mammalian members of the STE20 family. LOK phosphorylated itself as well as substrates such as myelin basic protein and histone IIA on serine and threonine residues but not on tyrosine residues, establishing LOK as a novel serine/threonine kinase. When coexpressed in COS7 cells with the known MAP kinase isoforms (ERK, JNK, and p38), LOK activated none of them in contrast to PAK- and GCK-related kinases. These results suggest that LOK could be involved in a novel signaling pathway in lymphocytes, which is distinct from the known MAP kinase cascades.

AB - We have identified a new gene, designated lok (lymphocyte-oriented kinase), that encodes a 966-amino acid protein kinase whose catalytic domain at the N terminus shows homology to that of the STE20 family members involved in mitogen-activated protein (MAP) kinase cascades. The non-catalytic domain of LOK does not have any similarity to that of other known members of the family. There is a proline-rich motif with Src homology region 3 binding potential, followed by a long coiled-coil structure at the C terminus. LOK is expressed as a 130-kDa protein, which was detected predominantly in lymphoid organs such as spleen, thymus, and bone marrow, in contrast to other mammalian members of the STE20 family. LOK phosphorylated itself as well as substrates such as myelin basic protein and histone IIA on serine and threonine residues but not on tyrosine residues, establishing LOK as a novel serine/threonine kinase. When coexpressed in COS7 cells with the known MAP kinase isoforms (ERK, JNK, and p38), LOK activated none of them in contrast to PAK- and GCK-related kinases. These results suggest that LOK could be involved in a novel signaling pathway in lymphocytes, which is distinct from the known MAP kinase cascades.

UR - http://www.scopus.com/inward/record.url?scp=0030982497&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030982497&partnerID=8YFLogxK

U2 - 10.1074/jbc.272.36.22679

DO - 10.1074/jbc.272.36.22679

M3 - Article

C2 - 9278426

AN - SCOPUS:0030982497

VL - 272

SP - 22679

EP - 22684

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 36

ER -