Cytokinetic failure and asynchronous nuclear division in BHK cells overexpressing a truncated protein-tyrosine-phosphatase.
نویسندگان
چکیده
Previous work has shown that a T-cell protein-tyrosine-phosphatase truncated in its carboxyl-terminal domain (delta C11.PTP) has full enzymatic activity but no longer localizes in the particulate fraction of the cell. Two baby hamster kidney (BHK) cell lines overexpressing the truncated protein are markedly multinucleate, a state likely caused by a failure in cytokinesis. Nuclei within syncytial cells overexpressing delta C11.PTP display a remarkable asynchronous entry into mitosis. The effects require tyrosine phosphatase activity because expression of an inactive form of the truncated enzyme yields cells indistinguishable from the parental cell line. Redistribution of the enzyme from the particulate to the soluble fraction is apparently important to these observed effects because cells overexpressing the full-length, wild-type enzyme are morphologically similar to controls. Further, when these cells contain more than one nucleus, their syncytial nuclei undergo mitosis synchronously.
منابع مشابه
PSTPIP: A Tyrosine Phosphorylated Cleavage Furrow–associated Protein that Is a Substrate for a PEST Tyrosine Phosphatase
We have investigated proteins which interact with the PEST-type protein tyrosine phosphatase, PTP hematopoietic stem cell fraction (HSCF), using the yeast two-hybrid system. This resulted in the identification of proline, serine, threonine phosphatase interacting protein (PSTPIP), a novel member of the actin- associated protein family that is homologous to Schizosaccharomyces pombe CDC15p, a ph...
متن کاملRegulation of fibroblast motility by the protein tyrosine phosphatase PTP-PEST.
The protein tyrosine phosphatase PTP-PEST is a cytosolic enzyme that displays a remarkable degree of selectivity for tyrosine-phosphorylated p130(Cas) as a substrate, both in vitro and in intact cells. We have investigated the physiological role of PTP-PEST using Rat1 fibroblast-derived stable cell lines that we have engineered to overexpress PTP-PEST. These cell lines exhibit normal levels of ...
متن کاملOverexpression of the transmembrane tyrosine phosphatase LAR activates the caspase pathway and induces apoptosis
BACKGROUND The protein tyrosine phosphatase family comprises transmembrane receptor-like and cytosolic forms. Although the exact biological functions of these enzymes are largely unknown, they are believed to counter-balance the effects of protein tyrosine kinases. We have previously identified and characterized a mammalian transmembrane protein tyrosine phosphatase, called LAR (leukocyte commo...
متن کاملG2/M arrest caused by actin disruption is a manifestation of the cell size checkpoint in fission yeast.
In budding yeast, actin disruption prevents nuclear division. This has been explained as activation of a morphogenesis checkpoint monitoring the integrity of the actin cytoskeleton. The checkpoint operates through inhibitory tyrosine phosphorylation of Cdc28, the budding yeast Cdc2 homolog. Wild-type Schizosaccharomyces pombe cells also arrest before mitosis after actin depolymerization. Oversi...
متن کاملEvidence that DIF-1 and hyper-osmotic stress activate a Dictyostelium STAT by inhibiting a specific protein tyrosine phosphatase.
STATc becomes tyrosine phosphorylated and accumulates in the nucleus when Dictyostelium cells are exposed to the prestalk cell inducer Differentiation inducing factor 1 (DIF-1), or are subjected to hyper-osmotic stress. We show that the protein tyrosine phosphatase PTP3 interacts directly with STATc and that STATc is refractory to activation in PTP3 overexpressing cells. Conversely, overexpress...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 89 12 شماره
صفحات -
تاریخ انتشار 1992