Hematopoietic cells express two forms of lyn kinase differing by 21 amino acids in the amino terminus.

Yi, Taolin; Bolen, Joseph B.; Ihle, James N.

doi:10.1128/mcb.11.5.2391

Cited by 145 publications

(89 citation statements)

References 36 publications

(40 reference statements)

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“…As an Src kinase member mainly expressed in B and myeloid lineages (Yi et al, 1991), it is plausible that Lyn phosphorylates and activates STAT in a JAK-independent manner. In support of this hypothesis, Lyn plays a role in erythropoietin-induced tyrosine phosphorylation of STAT5 (Okutani et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

Engagement of the B-cell antigen receptor activates STAT through Lyn in a Jak-independent pathway

2006

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Engagement of the B-cell antigen receptor (BCR) initiated by the Src kinase Lyn triggers rapid signaling cascades, leading to proliferation, differentiation or growth arrest of B cells. The Janus kinase (JAK)-STAT (signal transducer and activator of transcription) pathway, activated through cytokine receptors, mediates similar responses. Hypothesizing that Src and JAK pathways engage in crosstalk in B-cell signaling, we studied wild-type and Lyn-null B-cell lines, which express BCR. We found that activated BCR results in tyrosine phosphorylation of JAK-STAT, which required Lyn. To confirm that STAT activation is not due to JAK, we cloned the chicken homologs of JAK1 and JAK2 and made their antisense constructs. In cells expressing antisense JAK1 and JAK2, tyrosine phosphorylation of STAT was not inhibited following BCR stimulation. Using activation loop-specific phosphotyrosine antibodies, we did not detect phospho-JAK1 and phospho-JAK2 after BCR stimulation. The JAK inhibitor AG490 did not inhibit the tyrosine phosphorylation of Lyn or STAT after BCR simulation. An in vitro phosphorylation assay showed that Lyn directly phosphorylates STAT3. In an electrophoretic mobility shift assay, BCR stimulation led to enhanced DNA binding of the STAT3 in DT40, but not in the Lynnull cells. We conclude that BCR engagement activates the STAT pathway via Lyn, independent of JAK.

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Section: Discussionmentioning

confidence: 99%

Engagement of the B-cell antigen receptor activates STAT through Lyn in a Jak-independent pathway

2006

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“…Expression plasmids for various CrkL mutants were described previously (16). Expression plasmids for alternatively spliced isoforms of murine Lyn (pXM-LynA and pXM-LynB) have been described previously (5,23). An expression plasmid for a Lyn mutant (pXM-LynAN) in which a C-terminal half-portion of the kinase domain (amino acids 397-512) is deleted was constructed by introducing a stop codon by the polymerase chain reaction method, as described previously (5).…”

Section: Methodsmentioning

confidence: 99%

CrkL Is Recruited through Its SH2 Domain to the Erythropoietin Receptor and Plays a Role in Lyn-mediated Receptor Signaling

Arai¹,

Kanda²,

Nosaka³

et al. 2001

Journal of Biological Chemistry

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“…Concerning Lyn, the cDNA used in this experiment corresponds to the 56 kDa isoform of the kinase. Indeed, two isoforms of Lyn, p53 and p56 Lyn have been described that dier only in a short 21 amino-acids sequence located in the unique N-terminal region (Yi et al, 1991 …”

Section: Cleavage Of Src Kinases By Caspase 3 In Vitromentioning

confidence: 99%

Cleavage of Fyn and Lyn in their N-terminal unique regions during induction of apoptosis: a new mechanism for Src kinase regulation

2001

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Hematopoietic cells express two forms of lyn kinase differing by 21 amino acids in the amino terminus.

Cited by 145 publications

References 36 publications

Engagement of the B-cell antigen receptor activates STAT through Lyn in a Jak-independent pathway

Engagement of the B-cell antigen receptor activates STAT through Lyn in a Jak-independent pathway

CrkL Is Recruited through Its SH2 Domain to the Erythropoietin Receptor and Plays a Role in Lyn-mediated Receptor Signaling

Cleavage of Fyn and Lyn in their N-terminal unique regions during induction of apoptosis: a new mechanism for Src kinase regulation

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