scholarly journals ANKRD54 preferentially selects Bruton’s Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain library

PLoS ONE ◽  
2017 ◽  
Vol 12 (4) ◽  
pp. e0174909 ◽  
Author(s):  
Manuela O. Gustafsson ◽  
Dara K. Mohammad ◽  
Erkko Ylösmäki ◽  
Hyunseok Choi ◽  
Subhash Shrestha ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Sh3 Domain ◽  
Bruton’S Tyrosine Kinase ◽  
Bruton's Tyrosine Kinase ◽  
Src Homology 3 ◽  
Src Homology

Sab (SH3BP5), a novel mitochondria-localized JNK-interacting protein

2004 ◽  
Vol 32 (6) ◽  
pp. 1075-1077 ◽  
Author(s):  
C. Wiltshire ◽  
D.A.F. Gillespie ◽  
G.H.W. May
Keyword(s):  
Tyrosine Kinase ◽  
Protein Interactions ◽  
Bruton’S Tyrosine Kinase ◽  
Protein Protein Interactions ◽  
Bruton's Tyrosine Kinase ◽  
Interacting Protein ◽  
Subcellular Compartment ◽  
Cellular Processes ◽  
Mitogen Activated Protein ◽  
Src Homology

The JNK (c-Jun N-terminal kinase) pathway is activated by diverse stresses and can have an effect on a number of different cellular processes. Protein–protein interactions are critical for efficient signalling from JNK to multiple targets; through a screen for interacting proteins, we identified a novel JNK-interacting protein, Sab (SH3BP5). Sab has previously been found to interact with the Src homology 3 domain of Bruton's tyrosine kinase; however, the interaction with JNK occurs through a mitogen-activated protein KIM (kinase interaction motif) in a region distinct from the Bruton's tyrosine kinase-binding domain. As with c-Jun, the presence of this KIM is essential for Sab to act as a JNK substrate. Interestingly, Sab is associated with the mitochondria and co-localizes with a portion of active JNK after stress treatment. The present study and previously reported work may suggest a possible role for Sab in targeting JNK to this subcellular compartment and/or mediating crosstalk between different signal-transduction pathways.

scholarly journals Intermolecular interactions between the SH3 domain and the proline-rich TH region of Bruton's tyrosine kinase

FEBS Letters ◽  
2001 ◽  
Vol 489 (1) ◽  
pp. 67-70 ◽  
Author(s):  
Henrik Hansson ◽  
Michael P Okoh ◽  
C.I.Edvard Smith ◽  
Mauno Vihinen ◽  
Torleif Härd
Keyword(s):  
Tyrosine Kinase ◽  
Intermolecular Interactions ◽  
Sh3 Domain ◽  
Bruton’S Tyrosine Kinase ◽  
Bruton's Tyrosine Kinase

scholarly journals The protein product of the c-cbl protooncogene is phosphorylated after B cell receptor stimulation and binds the SH3 domain of Bruton's tyrosine kinase.

1995 ◽  
Vol 182 (2) ◽  
pp. 611-615 ◽  
Author(s):  
G O Cory ◽  
R C Lovering ◽  
S Hinshelwood ◽  
L MacCarthy-Morrogh ◽  
R J Levinsky ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
B Cell ◽  
Cell Receptor ◽  
Sh3 Domain ◽  
Protein Product ◽  
B Cell Receptor ◽  
Bruton’S Tyrosine Kinase ◽  
B Cell Differentiation ◽  
Receptor Stimulation ◽  
Bruton's Tyrosine Kinase

X-linked agammaglobulinemia, a B cell immunodeficiency, is caused by mutations in the Bruton's tyrosine kinase (Btk) gene. The absence of a functional Btk protein leads to a failure of B cell differentiation and antibody production. B cell receptor stimulation leads to the phosphorylation of the Btk protein and it is, therefore, likely that Btk is involved in B cell receptor signaling. As a nonreceptor tyrosine kinase, Btk is likely to interact with several proteins within the context of a signal transduction pathway. To understand such interactions, we have generated glutathione S-transferase fusion proteins corresponding to different domains of the human Btk protein. We have identified a 120-kD protein present in human B cells as being bound by the SH3 domain of Btk and which, after B cell receptor stimulation, is one of the major substrates of tyrosine phosphorylation. We have shown that this 120-kD protein is the protein product of c-cbl, a protooncogene, which is known to be phosphorylated in response to T cell receptor stimulation and to interact with several other tyrosine kinases. Association of the SH3 domain of Btk with p120cbl provides evidence for an analogous role for p120cbl in B cell signaling pathways. The p120cbl protein is the first identified ligand of the Btk SH3 domain.

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