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SHIP1, an SH2 Domain Containing Polyinositol-5-phosphatase, Regulates Migration through Two Critical Tyrosine Residues and Forms a Novel Signaling Complex with DOK1 and CRKL

Sattler, Martin, Verma, Shalini, Pride, Yuri B., Salgia, Ravi, Rohrschneider, Larry R., Griffin, James D.·2001·Journal of Biological Chemistry
DOI 10.1074/jbc.m006250200
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FIG. 1 SHIP1 and DOK1 form a complex in Ba/F3.p210 cells re-expressing SHIP1. A-C, SHIP1 expression was induced by doxycycline treatment of Ba/F3.p210.pTRE-SHIP cells. Lysates of untreated cells ( 2 ) or cells treated for 18 h with 1 m g/ml doxycycline ( 1 ) were used for precipitations. A, lysates of 20 3 10 6 Ba/F3.p210.pTRE and Ba/F3.p210.pTRE-SHIP cells were incubated with anti-SHIP1 and anti-DOK1 antibodies and SHIP1, DOK1, or tyrosine-phosphorylated proteins were detected by immunoblotting ( I.B .). B, lysates of 20 3 10 6 Ba/ F3.p210.pTRE-SHIP cells were incubated with 5 m g of GST and GST fusion protein of the SHIP1 SH2 or the DOK1 PTB domain immobilized on glutathione beads. Co-precipitation of ABL, SHIP1, or DOK1 was detected by immunoblotting ( I.B .). C, lysates of 20 3 10 6 Ba/F3.p210.pTRE-SHIP cells were immunoprecipitated with antibodies against SHIP1, DOK1, and BCR/ABL as indicated. Proteins were separated by SDS-PAGE and transferred to nitrocellulose membrane. Specific direct binding of GST and a GST fusion protein of the DOK1 PTB domain or the SHIP1 SH2 domain to proteins in the immunoprecipitates was detected in a protein overlay assay. The molecular mass of the proteins is indicated in kDa on the left of each figure. D, Ba/F3.p210.TetON cell were transfected with the empty vector (pTRE), a vector containing full-length SHIP1 (pTRE-SHIP), or SHIP1 containing a Y917F (pTRE-SHIP.Y917F) or a Y1020F (pTRE-SHIP.Y1020F) point mutation. SHIP1 protein was induced 1 day after transfectionly by doxycycline treatment for 24 h. SHIP1 expression was detected by immunoblotting ( I.B .) in whole cell lysate (2.5 3 10 5 cells) or in precipitations using a GST-DOK1 PTB domain fusion protein and lysates of 25 3 10 6 cells. The molecular mass of the proteins is as indicated in kDa on the left of each figure.
FIG. 1 SHIP1 and DOK1 form a complex in Ba/F3.p210 cells re-expressing SHIP1. A-C, SHIP1 expression was induced by doxycycline treatment of Ba/F3.p210.pTRE-SHIP cells. Lysates of untreated cells ( 2 ) or cells treated for 18 h with 1 m g/ml doxycycline ( 1 ) were used for precipitations. A, lysates of 20 3 10 6 Ba/F3.p210.pTRE and Ba/F3.p210.pTRE-SHIP cells were incubated with anti-SHIP1 and anti-DOK1 antibodies and SHIP1, DOK1, or tyrosine-phosphorylated proteins were detected by immunoblotting ( I.B .). B, lysates of 20 3 10 6 Ba/ F3.p210.pTRE-SHIP cells were incubated with 5 m g of GST and GST fusion protein of the SHIP1 SH2 or the DOK1 PTB domain immobilized on glutathione beads. Co-precipitation of ABL, SHIP1, or DOK1 was detected by immunoblotting ( I.B .). C, lysates of 20 3 10 6 Ba/F3.p210.pTRE-SHIP cells were immunoprecipitated with antibodies against SHIP1, DOK1, and BCR/ABL as indicated. Proteins were separated by SDS-PAGE and transferred to nitrocellulose membrane. Specific direct binding of GST and a GST fusion protein of the DOK1 PTB domain or the SHIP1 SH2 domain to proteins in the immunoprecipitates was detected in a protein overlay assay. The molecular mass of the proteins is indicated in kDa on the left of each figure. D, Ba/F3.p210.TetON cell were transfected with the empty vector (pTRE), a vector containing full-length SHIP1 (pTRE-SHIP), or SHIP1 containing a Y917F (pTRE-SHIP.Y917F) or a Y1020F (pTRE-SHIP.Y1020F) point mutation. SHIP1 protein was induced 1 day after transfectionly by doxycycline treatment for 24 h. SHIP1 expression was detected by immunoblotting ( I.B .) in whole cell lysate (2.5 3 10 5 cells) or in precipitations using a GST-DOK1 PTB domain fusion protein and lysates of 25 3 10 6 cells. The molecular mass of the proteins is as indicated in kDa on the left of each figure.CC-BY-NC-ND · From the PDF
FIG. 2 SHIP1 and CRKL form a complex in Ba/F3.p210 cells re-expressing SHIP1. A-C, SHIP1 expression was induced by doxycycline treatment of Ba/F3.p210.pTRE-SHIP cells. Lysates of untreated cells ( 2 ) or cells treated for 18 h with 1 m g/ml doxycycline ( 1 ) were used for precipitations. The molecular mass of the proteins is indicated in kDa on the left of each figure. A, lysates of 20 3 10 6 Ba/F3.p210.pTRESHIP and Ba/F3.p210.pTRE-SHIP cells were incubated with antiCRKL antibodies and SHIP, CRKL, or p85 PI3K (PI3K) protein detected by immunoblotting ( I.B .). B, lysates of 20 3 10 6 Ba/F3.p210.pTRE-SHIP cells were incubated with 5 m g of GST and GST fusion protein of the CRKL SH2 or the CRKL SH3 domain immobilized on glutathione beads. Co-precipitation of SHIP, CBL, or p85 PI3K (PI3K) was detected by immunoblotting ( I.B .). C, lysates of 20 3 10 6 Ba/F3.p210.pTRE-SHIP cells were immunoprecipitated with antibodies against SHIP1 and CBL as indicated. Proteins were separated by SDS-PAGE, and transferred to polyvinylidene difluoride membrane. Specific direct binding of GST and a GST fusion protein of the CRKL SH2 domain to proteins in the immunoprecipitates was detected in a protein overlay assay.
FIG. 2 SHIP1 and CRKL form a complex in Ba/F3.p210 cells re-expressing SHIP1. A-C, SHIP1 expression was induced by doxycycline treatment of Ba/F3.p210.pTRE-SHIP cells. Lysates of untreated cells ( 2 ) or cells treated for 18 h with 1 m g/ml doxycycline ( 1 ) were used for precipitations. The molecular mass of the proteins is indicated in kDa on the left of each figure. A, lysates of 20 3 10 6 Ba/F3.p210.pTRESHIP and Ba/F3.p210.pTRE-SHIP cells were incubated with antiCRKL antibodies and SHIP, CRKL, or p85 PI3K (PI3K) protein detected by immunoblotting ( I.B .). B, lysates of 20 3 10 6 Ba/F3.p210.pTRE-SHIP cells were incubated with 5 m g of GST and GST fusion protein of the CRKL SH2 or the CRKL SH3 domain immobilized on glutathione beads. Co-precipitation of SHIP, CBL, or p85 PI3K (PI3K) was detected by immunoblotting ( I.B .). C, lysates of 20 3 10 6 Ba/F3.p210.pTRE-SHIP cells were immunoprecipitated with antibodies against SHIP1 and CBL as indicated. Proteins were separated by SDS-PAGE, and transferred to polyvinylidene difluoride membrane. Specific direct binding of GST and a GST fusion protein of the CRKL SH2 domain to proteins in the immunoprecipitates was detected in a protein overlay assay.CC-BY-NC-ND · From the PDF
FIG. 4 Tyr 917 and Tyr 1020 in SHIP1 regulate spontaneous Transwell migration. A and B, Ba/F3.p210.TetON cells transfected with a wild type SHIP1 expression vector (pTRE-SHIP) and vectors containing the SHIP1 mutants Y917F (pTRE-SHIP.Y917F) or Y1020F (pTRE-SHIP.Y1020F) were either left untreated ( 2 ) or treated with doxycycline ( 1 ) and used for immunoblotting ( I.B .) or Transwell migration. A, expression of wild type SHIP1 and the two SHIP1 mutants was detected in total cell lysates (2.5 3 10 5 cells) by immunoblotting ( I.B .) with anti-SHIP1 antibodies. The blot was stripped and reprobed with anti-PI3K antibodies. The molecular mass of the proteins is indicated in kDa on the left of the figure. B, cells were used for Transwell migration assays and the number of viable cells in the lower chamber was determined after 2.5 h. The change in migration of four independent experiments was calculated as a migration index. The error bars indicate the standard error of the mean. The p values were calculated and a significant decrease ( p , 0.01) indicated by an asterisk (*).
FIG. 4 Tyr 917 and Tyr 1020 in SHIP1 regulate spontaneous Transwell migration. A and B, Ba/F3.p210.TetON cells transfected with a wild type SHIP1 expression vector (pTRE-SHIP) and vectors containing the SHIP1 mutants Y917F (pTRE-SHIP.Y917F) or Y1020F (pTRE-SHIP.Y1020F) were either left untreated ( 2 ) or treated with doxycycline ( 1 ) and used for immunoblotting ( I.B .) or Transwell migration. A, expression of wild type SHIP1 and the two SHIP1 mutants was detected in total cell lysates (2.5 3 10 5 cells) by immunoblotting ( I.B .) with anti-SHIP1 antibodies. The blot was stripped and reprobed with anti-PI3K antibodies. The molecular mass of the proteins is indicated in kDa on the left of the figure. B, cells were used for Transwell migration assays and the number of viable cells in the lower chamber was determined after 2.5 h. The change in migration of four independent experiments was calculated as a migration index. The error bars indicate the standard error of the mean. The p values were calculated and a significant decrease ( p , 0.01) indicated by an asterisk (*).CC-BY-NC-ND · From the PDF

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Metadata

Authors
Sattler, M., Verma, S., Pride, Y. B., Salgia, R., Rohrschneider, L. R., & Griffin, J. D.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2001-01
Volume
276
Issue
4
Pages
2451-2458
ISSN
0021-9258
DOI
10.1074/jbc.m006250200
Cited by
46
References
2
Language
en
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