Localization and function of tyrosine-phosphorylated protein in pig oocytes.
Several proteins with phosphorylated tyrosine residues have been shown to be closely involved in the control meiotic nuclear division. We identified a 42-kD protein in pig oocytes, using a polyclonal antibody to a synthetic phosphotyrosine construct that increases significantly in amount after 12 hr of maturation culture, and is discretely localized to condensing and condensed chromosomes. However, since microinjection of the antibody into oocytes blocks spindle formation, the role of this protein appears to be at that stage rather than directly in chromosome condensation. Specificity of action of the 42-kD protein indicates that it may be a phosphorylation-dependent component necessary for successful spindle assembly.
Miyano
T
T
Department of Development and Signalling, Babraham Institute, Cambridge, UK.
Moor
R M
RM
Wooding
F B
FB
Shiroo
M
M
D000818:Animals; D005260:Female; D007150:Immunohistochemistry; D008540:Meiosis; D008845:Microinjections; D009865:Oocytes / Q000378:metabolism; D010053:Ovary / Q000166:cytology / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011817:Rabbits; D013552:Swine / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism
D010750:Phosphoproteins; D014443:Tyrosine