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an important role for Cas proteins in cell-cell adhesion signaling in development
serum phospho-CSE1L is useful for early detecting the efficacy of targeted therapy in initial treatment.
CSE1L knockdown reduced Ras-induced metastasis of B16F10 melanoma cells in C57BL/ (show HRAS Proteins)6 mice. v-H-Ras expression altered the cellular trafficking of CSE1L and increased CSE1L secretion.
Serum cellular apoptosis susceptibility protein may have a role in progression of metastatic colorectal cancer
CSE1L/CAS has a role in proliferation and apoptosis [review]
Cse1l is a negative regulator of cystic fibrosis transmembrane conductance regulator (show CFTR Proteins)-dependent fluid secretion.
Our data suggest a previously unanticipated link between CAS and integrin beta1 signaling which correlates with an aggressive hepatocellular carcinoma phenotype.
CSE1L knockdown by shRNA inhibited protein, resulting in decreased cell proliferation, reduced colony formation in soft agar, and induction of apoptosis. CSE1L protein is expressed early and across all stages of colorectal carcinoma (CRC (show CALR Proteins)) development. shRNA knockdown of CSE1L was associated with inhibition of tumorigenesis in CRC (show CALR Proteins) cells. CSE1L may represent a potential target for treatment of CRC (show CALR Proteins).
Data suggest that CAS overexpression in thyroid carcinoma depends on the subtype and the disease stage. Our findings also indicate that CAS maintains papillary thyroid cell proliferation and survival.
There is a relationship between nuclear CSE1L overexpression and distant metastasis in breast cancer.
CAS plays contrasting roles in proliferation and apoptosis
hCAS/CSE1L is responsible for controlling the homologous recombinational repair activity by directly interacting with RAD51 (show RAD51 Proteins).
nuclear CSE1L is mainly non-phosphorylated CSE1L and is involved in gene regulation and cytoplasmic CSE1L is mainly phosphorylated CSE1L and is involved in cytoplasmic signaling regulation in melanocytic tumorigenesis.
These results indicate that CSE1L is associated with viability and apoptosis, cellular adhesion and invasion, thus implicating CSE1L in the progression of colorectal cancer.
The cellular apoptosis susceptibility/importin-alpha1 transport cycle is linked to X-linked inhibitor (XIAP (show XIAP Proteins)) and is required to maintain tumor cell survival in hepatocellular carcinoma.
CSE1L expression was significantly inhibited in RKO cells, causing cell cycle arrest in the G2/M and S phases and a delay in cell proliferation, as well as induction of apoptosis and an inhibition of colony growth capacity.
Proteins that carry a nuclear localization signal (NLS) are transported into the nucleus by the importin-alpha/beta heterodimer. Importin-alpha binds the NLS, while importin-beta mediates translocation through the nuclear pore complex. After translocation, RanGTP binds importin-beta and displaces importin-alpha. Importin-alpha must then be returned to the cytoplasm, leaving the NLS protein behind. The protein encoded by this gene binds strongly to NLS-free importin-alpha, and this binding is released in the cytoplasm by the combined action of RANBP1 and RANGAP1. In addition, the encoded protein may play a role both in apoptosis and in cell proliferation. Alternatively spliced transcript variants have been found for this gene.
, Importin-alpha re-exporter
, CSE1 chromosome segregation 1-like (yeast)
, CSE1 chromosome segregation 1-like protein
, CSE1 chromosome segregation 1-like
, chromosome segregation 1-like protein
, importin-alpha re-exporter
, cellular apoptosis susceptibilit
, cellular apoptosis susceptibility
, exportin 2
, cellular apoptosis susceptibility protein