Detection of a novel mutation in the SRC homology domain 2 (SH2) of Bruton's tyrosine kinase and direct female carrier evaluation in a family with X-linked agammaglobulinemia

1996 ◽  
Vol 63 (1) ◽  
pp. 318-322 ◽  
Author(s):  
Volker Schuster ◽  
Silvia Seidenspinner ◽  
Hans Wolfgang Kreth
Keyword(s):  
Tyrosine Kinase ◽  
Novel Mutation ◽  
Female Carrier ◽  
Bruton’S Tyrosine Kinase ◽  
Bruton's Tyrosine Kinase ◽  
Src Homology

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

scholarly journals A Novel Mutation (Cys145→Stop) in Bruton’s Tyrosine Kinase Is Associated with Newly Diagnosed X-Linked Agammaglobulinemia in a 51-Year-Old Male

1996 ◽  
Vol 2 (5) ◽  
pp. 619-623 ◽  
Author(s):  
Stephen J. Kornfeld ◽  
Robert N. Haire ◽  
Scott J. Strong ◽  
Huayang Tang ◽  
Sun-Sang J. Sung ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Novel Mutation ◽  
Bruton’S Tyrosine Kinase ◽  
Newly Diagnosed ◽  
Bruton's Tyrosine Kinase

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.

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