Dynamic phosphorylation/dephosphorylation is key to proper cell cycle control in that: (select all answers that apply)
A. |
CAKs phosphorylate (and activate) CDK subunits. |
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B. |
Wee1 kinase phosphorylates (and activates) CDK subunits. |
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C. |
Cdc25 kinase phosphorylates (and activates) CDK subunits. |
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D. |
Phosphorylation of the CKI Sic1 directs its subsequent ubiquitination and proteasomal degradation. |
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E. |
Kinases phosphorylate (and activate) SCF, the ubiquitin ligase responsible for degradation of G1/S phase cyclins. |
The correct answers are:
Kinases phosphorylate (and activate) SCF, the ubiquitin ligase responsible for degradation of G1/S phase cyclins.
CAKs phosphorylate (and activate) CDK subunits..
Mostly the cyclin CDK complexes regulate the cell cycle. Animals containing CDK 1, 2, 3 are directly involved in the regulation of cell cycle. These complexes phosphorylate substrates that are involved in cell cycle. The CAK 1 is a monomeric protein complex consisting of Cak1. It phosphorylates the Cdk and is responsible for its activation. The Skp-1 or SCf type E3 ubiquitin ligase complex is responsible for regulating the cellular level of ubiquitylation and proteolysis. SCF complexes are implicated in G1 - S progression, and anaphase promoting complex which are required for the separation of sister chromatids at anaphase and exit from Mphase into G1.
Dynamic phosphorylation/dephosphorylation is key to proper cell cycle control in that: (select all answers that apply)...
Phosphorylation-dependent binding of F-box protein B-TrCP containing E3 ubiquitin ligase to human WEE1A. S123 is phosphorylated by a CDK and the phosphorylation primes CK2 to phosphorylate S121 resulting in creation of a B-TCP phosphodegron (EEGFGpS121) that is responsible for the instability of WEE1A during interphase. At the onset of M-phase, when activated Plk1 accumulates, Plk1 binds to WEE1A to the PBD binding motif surrounding PS123 (SpSP) via its PBD and phosphorylates S53 resulting in generation of the second phosphodegron (DpSAFQE)....