Cyclin Dependent Kinase Inhibitor 1c
Cyclin Dependent Kinase Inhibitor 1c - Related Videos
12:26
Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Cited by 10 •
2018
Cyclin-dependent kinase 1 (Cdk1) is activated in the G2 phase of the cell cycle and regulates many cellular pathways. Here, we present a protocol for an in vitro kinase assay with Cdk1, which allows the identification of Cdk1-specific phosphorylation sites for establishing cellular targets of this important kinase.
10:49
Pre-clinical Evaluation of Tyrosine Kinase Inhibitors for Treatment of Acute Leukemia
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Cited by 6 •
2013
Receptor tyrosine kinases are ectopically expressed in many cancers and have been identified as therapeutic targets in acute leukemia. This manuscript describes an efficient strategy for pre-clinical evaluation of tyrosine kinase inhibitors for the treatment of acute leukemia.
06:42
Identifying Kinase Inhibitors that Modulate the Thymocyte Response to Strong TCR Signals
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2025
In this video, we describe a method to identify the small-molecule kinase inhibitors that modulate the apoptosis of self-reactive CD4+CD8+ double-positive immature thymocytes. Apoptosis is induced in the double-positive thymocytes by activating them with anti-CD3- and anti-CD28-coated magnetic beads; this is followed by a small-molecule inhibitor treatment and flow cytometry analysis to detect if the inhibitors modulate the apoptotic marker expression.
07:18
A Simple Method to Identify Kinases That Regulate Embryonic Stem Cell Pluripotency by High-throughput Inhibitor Screening
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Cited by 4 •
2017
Here, we present a quantitative and scalable protocol to perform targeted small molecule screens for kinase regulators of the naïve-primed pluripotent transition.
01:25
cAMP-dependent Protein Kinase Pathways
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2023
Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
FAQs
CDKN1C restrains kinase activity by associating with cyclin-dependent kinase complexes that contain CDK2 or CDK4/6. Lower kinase activity reduces phosphorylation of targets needed for G1-to-S progression. The key consequence is that cells face less molecular drive to enter the DNA-synthesis phase, connecting inhibitor function with control of cellular proliferation.
Regulating entry into S phase does more than limit cell multiplication. It helps coordinate cellular proliferation with differentiation, tissue growth, and developmental patterning. For CDKN1C, this makes cell-cycle inhibition relevant to the formation and organization of developing tissues, rather than treating proliferation as an isolated process.
Because CDKN1C is maternally expressed and imprinted, its activity is studied in the context of regulated gene expression linked to developmental growth. This feature connects CDKN1C regulation with tissue patterning and helps explain why altered control of its function is relevant to congenital overgrowth disorders.
Studies of these disorders can connect abnormal tissue growth with changes in a specific cell-cycle inhibitory pathway. Investigators can use CDKN1C regulation and function to examine how impaired restraint of CDK2- or CDK4/6-associated activity might contribute to excessive growth and altered developmental patterning.
Its normal function provides a reference point for understanding cancers in which cell-cycle inhibition is disrupted. When the restraint associated with CDKN1C is weakened, proliferation can become less controlled. Research therefore examines this pathway to relate altered inhibition to failure of tumor-suppressive control and cancer-associated growth.
CDKN1C offers a way to study how cell-cycle restraint intersects with decisions about proliferation and differentiation. Because the protein links these processes with tissue growth and developmental patterning, investigators can examine how altered inhibitory regulation may influence stem-cell behavior within broader developmental contexts.