» Articles » PMID: 15888917

Focal Adhesion Kinase-related Protein Tyrosine Kinase Pyk2 in T-cell Activation and Function

Overview
Journal Immunol Res
Date 2005 May 13
PMID 15888917
Citations 19
Authors
Affiliations
Soon will be listed here.
Abstract

Pyk2 is a protein tyrosine kinase expressed primarily in brain and hematopoietic cells. It becomes activated in response to stimulation through numerous receptors, including integrins, chemokine receptors, and antigen receptors, and is found in association with src-family kinases. Although this enzyme associates with many proteins known to be important for activation and has many characteristics of a scaffolding protein, its function remains elusive. A number of studies in non-T-cells suggest that Pyk2 is important for cell spreading, cell migration, and integrin function; however, a defined role in T-cells has not been established. Here, we discuss evidence that implicates Pyk2 in directionality of signaling, which is essential to establishment of the directional killing mediated by cytotoxic lymphocytes.

Citing Articles

The integrin adhesome and control of anti-tumour immunity.

Webb E, Black A, Barth N, Symeonides S, Brunton V Biochem Soc Trans. 2024; 52(6):2455-2468.

PMID: 39641590 PMC: 11777417. DOI: 10.1042/BST20240386.


Identification of a Novel Serological Marker in Seronegative Rheumatoid Arthritis Using the Peptide Library Approach.

Bason C, Barbieri A, Martinelli N, Olivieri B, Argentino G, Bartoloni E Front Immunol. 2021; 12:753400.

PMID: 34675934 PMC: 8525329. DOI: 10.3389/fimmu.2021.753400.


How the Discovery of the CD4/CD8-p56 Complexes Changed Immunology and Immunotherapy.

Rudd C Front Cell Dev Biol. 2021; 9:626095.

PMID: 33791292 PMC: 8005572. DOI: 10.3389/fcell.2021.626095.


Proline-Rich Protein Tyrosine Kinase 2 in Inflammation and Cancer.

Zhu X, Bao Y, Guo Y, Yang W Cancers (Basel). 2018; 10(5).

PMID: 29738483 PMC: 5977112. DOI: 10.3390/cancers10050139.


Glycerol monolaurate induces filopodia formation by disrupting the association between LAT and SLP-76 microclusters.

Zhang M, Tran P, Wolff A, Tremblay M, Fosdick M, Houtman J Sci Signal. 2018; 11(528).

PMID: 29717064 PMC: 6048963. DOI: 10.1126/scisignal.aam9095.


References
1.
Sotsios Y, Ward S . Phosphoinositide 3-kinase: a key biochemical signal for cell migration in response to chemokines. Immunol Rev. 2001; 177:217-35. DOI: 10.1034/j.1600-065x.2000.17712.x. View

2.
Rodriguez-Fernandez J, Gomez M, Luque A, Hogg N, Sanchez-Madrid F, Cabanas C . The interaction of activated integrin lymphocyte function-associated antigen 1 with ligand intercellular adhesion molecule 1 induces activation and redistribution of focal adhesion kinase and proline-rich tyrosine kinase 2 in T lymphocytes. Mol Biol Cell. 1999; 10(6):1891-907. PMC: 25386. DOI: 10.1091/mbc.10.6.1891. View

3.
Li X, Hunter D, Morris J, Haskill J, Earp H . A calcium-dependent tyrosine kinase splice variant in human monocytes. Activation by a two-stage process involving adherence and a subsequent intracellular signal. J Biol Chem. 1998; 273(16):9361-4. DOI: 10.1074/jbc.273.16.9361. View

4.
Park S, Avraham H, Avraham S . RAFTK/Pyk2 activation is mediated by trans-acting autophosphorylation in a Src-independent manner. J Biol Chem. 2004; 279(32):33315-22. DOI: 10.1074/jbc.M313527200. View

5.
Watson J, Harding T, Golubovskaya V, Morris J, Hunter D, Li X . Inhibition of the calcium-dependent tyrosine kinase (CADTK) blocks monocyte spreading and motility. J Biol Chem. 2000; 276(5):3536-42. DOI: 10.1074/jbc.M006916200. View