SHIP2 (SH2 Domain-containing Inositol Phosphatase 2) SH2 Domain Negatively Controls SHIP2 Monoubiquitination in Response to Epidermal Growth Factor

The role of the inositol polyphosphate 5-phosphatases in cellular function and human disease

(2009) Lisa M. Ooms et al.   BIOCHEMICAL JOURNAL

Specific Tyrosine Phosphorylations Mediate Signal-Dependent Stimulation of SHIP2 Inositol Phosphatase Activity, while the SH2 Domain Confers an Inhibitory Effect To Maintain the Basal Activity

(2009) Nagendra K. Prasad et al.   BIOCHEMISTRY

Mutations in Phosphoinositide Metabolizing Enzymes and Human Disease

(2009) Heather J. McCrea et al.   PHYSIOLOGY

Crucial role of the C-terminus of PTEN in antagonizing NEDD4-1-mediated PTEN ubiquitination and degradation

(2008) Xinjiang Wang et al.   BIOCHEMICAL JOURNAL

Differential regulation of the two transcriptional activation domains of the coiled-coil coactivator CoCoA by sumoylation

(2008) Catherine K Yang et al.   BMC MOLECULAR BIOLOGY

The docking properties of SHIP2 influence both JIP1 tyrosine phosphorylation and JNK activity

(2008) Jingwei Xie et al.   CELLULAR SIGNALLING

Hepatocyte Growth Factor, but not Vascular Endothelial Growth Factor, Attenuates Angiotensin II–Induced Endothelial Progenitor Cell Senescence

(2008) Fumihiro Sanada et al.   HYPERTENSION

The ubiquitin ligase Nedd4-1 is dispensable for the regulation of PTEN stability and localization

(2008) F. Fouladkou et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA