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ABL1 — JAK2
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Hprd Interaction:
JAK2
—
ABL1
(in vitro)
Xie et al., Oncogene 2001*, Argetsinger et al., Mol Cell Biol 2004, Feng et al., Mol Cell Biol 1997
-
IRef Hprd Interaction:
JAK2
—
ABL1
(in vivo)
Xie et al., Oncogene 2001*, Argetsinger et al., Mol Cell Biol 2004, Feng et al., Mol Cell Biol 1997
Text-mined interactions from Literome
Xie et al., Oncogene 2001
:
Moreover, tyrosine phosphorylation of
Jak2 by Bcr-Abl was
inhibited by the
Abl tyrosine kinase inhibitor, STI 571, in a dose dependent manner
Xie et al., Oncogene 2002
(Leukemia, Myelogenous, Chronic, BCR-ABL Positive) :
Since the Jak2 binds to the C-terminal domain of
Bcr-Abl and optimal
Jak2 activation requires the SH2 domain, we tested whether Jak2 was involved in c-Myc protein induction by Bcr-Abl
Limnander et al., Mol Cell 2004
(Cell Transformation, Neoplastic) :
SOCS-1 is expressed in v-Abl transformed cells but is unable to inhibit
v-Abl mediated
Jak-Stat signaling
Zhou et al., J Exp Med 2008
(Cell Transformation, Neoplastic...) :
Interestingly, coexpression of Ahi-1 in BCR-ABL-inducible cells reverses growth deficiencies exhibited by BCR-ABL down-regulation and is associated with sustained phosphorylation of
BCR-ABL and enhanced
activation of
JAK2-STAT5
Samanta et al., Leukemia 2011
(Leukemia, Myelogenous, Chronic, BCR-ABL Positive) :
Janus kinase 2 regulates
Bcr-Abl signaling in chronic myeloid leukemia ... Knocking down
Jak2 in Bcr-Abl+ cells
reduced levels of the
Bcr-Abl protein and also the phosphorylation of Tyr177 of Bcr-Abl, and Jak2 overexpression rescued these knockdown effects ... Importantly,
Jak2 inhibition decreased pTyr177 Bcr-Abl in immune complexes but did not
reduce levels of
Bcr-Abl , suggesting that the reduction of Bcr-Abl by Jak2 inhibition is a separate event from phosphorylation of Tyr177
Wilson-Rawls et al., Leukemia 1997
:
P210
Bcr-Abl interacts with the interleukin-3 beta c subunit and constitutively
activates Jak2