Cell cycle-dependent association of Gag-Mil and hsp90

Josip Lovrić; Oliver Bischof; Karin Moelling

doi:10.1016/0014-5793(94)80598-9

Cell cycle-dependent association of Gag-Mil and hsp90

Josip Lovrić, Oliver Bischof, Karin Moelling

Research output: Contribution to journal › Article › peer-review

Abstract

Immunoprecipitated p100Gag-Mil protein kinase from MH2-transformed quail embryo fibroblasts is associated with an 89 kDa protein. The molar ratio between p89 and Gag-Mil in the immunocomplex is 0.72, indicating that the majority of Gag-Mil is complexed with p89. During mitosis part of Gag-Mil is shifted to a form with reduced electrophoretic mobility, p102Gag-Mil. Appearance of p102Gag-Mil leads to a reduced association with p89 indicating that p102 is not associated with p89. Microsequencing of p89 isolated from immunoprecipitates of Gag-Mil identified the protein as the quail homologue of chicken hsp90. Our results show that p100Gag-Mil is associated with hsp90 with a high stoichiometry and that upshifted p102Gag-Mil is released from the complex with hsp90. © 1994.

Original language	English
Pages (from-to)	15-21
Number of pages	6
Journal	FEBS Letters
Volume	343
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(94)80598-9
Publication status	Published - 18 Apr 1994

Keywords

c-Raf-1
Cell cycle
Gag-Mil
hsp90
Microsequencing

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10.1016/0014-5793(94)80598-9

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title = "Cell cycle-dependent association of Gag-Mil and hsp90",

abstract = "Immunoprecipitated p100Gag-Mil protein kinase from MH2-transformed quail embryo fibroblasts is associated with an 89 kDa protein. The molar ratio between p89 and Gag-Mil in the immunocomplex is 0.72, indicating that the majority of Gag-Mil is complexed with p89. During mitosis part of Gag-Mil is shifted to a form with reduced electrophoretic mobility, p102Gag-Mil. Appearance of p102Gag-Mil leads to a reduced association with p89 indicating that p102 is not associated with p89. Microsequencing of p89 isolated from immunoprecipitates of Gag-Mil identified the protein as the quail homologue of chicken hsp90. Our results show that p100Gag-Mil is associated with hsp90 with a high stoichiometry and that upshifted p102Gag-Mil is released from the complex with hsp90. {\textcopyright} 1994.",

keywords = "c-Raf-1, Cell cycle, Gag-Mil, hsp90, Microsequencing",

author = "Josip Lovri{\'c} and Oliver Bischof and Karin Moelling",

year = "1994",

month = apr,

day = "18",

doi = "10.1016/0014-5793(94)80598-9",

language = "English",

volume = "343",

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journal = "FEBS Letters",

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TY - JOUR

T1 - Cell cycle-dependent association of Gag-Mil and hsp90

AU - Lovrić, Josip

AU - Bischof, Oliver

AU - Moelling, Karin

PY - 1994/4/18

Y1 - 1994/4/18

N2 - Immunoprecipitated p100Gag-Mil protein kinase from MH2-transformed quail embryo fibroblasts is associated with an 89 kDa protein. The molar ratio between p89 and Gag-Mil in the immunocomplex is 0.72, indicating that the majority of Gag-Mil is complexed with p89. During mitosis part of Gag-Mil is shifted to a form with reduced electrophoretic mobility, p102Gag-Mil. Appearance of p102Gag-Mil leads to a reduced association with p89 indicating that p102 is not associated with p89. Microsequencing of p89 isolated from immunoprecipitates of Gag-Mil identified the protein as the quail homologue of chicken hsp90. Our results show that p100Gag-Mil is associated with hsp90 with a high stoichiometry and that upshifted p102Gag-Mil is released from the complex with hsp90. © 1994.

AB - Immunoprecipitated p100Gag-Mil protein kinase from MH2-transformed quail embryo fibroblasts is associated with an 89 kDa protein. The molar ratio between p89 and Gag-Mil in the immunocomplex is 0.72, indicating that the majority of Gag-Mil is complexed with p89. During mitosis part of Gag-Mil is shifted to a form with reduced electrophoretic mobility, p102Gag-Mil. Appearance of p102Gag-Mil leads to a reduced association with p89 indicating that p102 is not associated with p89. Microsequencing of p89 isolated from immunoprecipitates of Gag-Mil identified the protein as the quail homologue of chicken hsp90. Our results show that p100Gag-Mil is associated with hsp90 with a high stoichiometry and that upshifted p102Gag-Mil is released from the complex with hsp90. © 1994.

KW - c-Raf-1

KW - Cell cycle

KW - Gag-Mil

KW - hsp90

KW - Microsequencing

U2 - 10.1016/0014-5793(94)80598-9

DO - 10.1016/0014-5793(94)80598-9

M3 - Article

VL - 343

SP - 15

EP - 21

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Cell cycle-dependent association of Gag-Mil and hsp90

Abstract

Keywords

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