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Question about Cell signaling

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CA2+, IP3, and cAMP have all been described as second messengers. In what ways are their mechanisms of action similar? In what ways are they different? If you were comparing the molecular structure of kinesin and dynein, which part (heads or tails) would you expect to be most similar between them? Why?

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This question can present itself to be quite engrossing with regard to the details you may get bogged down in. The focus should involve characteristic aspects for the Ca++, IP3, and cAMP second messengers:
1)Composition
Make specific distinctions regarding the three second messengers.
Calcium is an ion where-as cAMP is a biomolecule (protein) and a derivative of ATP (the bodies inherent energy source).
2)Origin
These second messengers and their method of actions can be dependent on their origin. For example G-protein coupled receptors can either activate (Gs-protein) or inhibit (Gi-protein) Adenylate cyclase. Adenylate cyclase is the enzyme catalyzing the reaction to form cAMP from ATP. This would differ from Ca++ as a second messenger which may act as a second messenger ...

Solution Summary

The solution analyzed CA2+, IP3, and cAMP's mechanisms and determines which actions are similar and which actions are different.

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Cell Biology Multiple Choice questions

1. Protein insertion into the mammalian ER membrane is typically
a. cotranslational c. pretranslational
b. post-translational d. quasitranslational

2. In N-glycosylation of proteins in the ER lumen, sugar(s) are added to the nascent chain at once.
a. 1 c. 7
b. 3 d. 14

3. All of the following proteins interact with exposed amino acids during protein folding in the ER except:
a. BiP c. PDI (protein disulfide isomerase)
b. calnexin and calreticulin d. prolylisomerase

4. Type I membrane proteins have all of the following properties except:
a. cleavable signal sequence c. internal stop-transfer sequence
b. internal signal-anchor sequence d. N-out, C-in topology

5. Proteins that do not fold properly in the ER lumen are degraded in the cytosol by
a. the etiosome c. the proteasome
b. the microsome d. the ribosome

6. Sorting of protein to mitochondrian and chloroplasts is
a. cotranslational c. pretranslational
b. post-translational d. quasitranslational

7. Tom/Tim and Toc/Tic protein complexes are involved in
a. post-receptor recognition events in the cytosolic folding of proteins prior to import into mitochondria or chloroplasts
b. pre-proteasomal steps in tagging aged proteins for degradation
c. protein translocation into mitochondria and chloroplasts, respectively
d. resetting biological clocks following rounds of intense protein synthesis

8. Protein sequences for targeting to mitochondria or chloroplasts are located at
a. the C-terminus of the precursor protein
b. amino acid position 173 in most mitochondrial and chloroplast proteins
c. the N-terminus of the precursor protein
d. At neither terminus.

9. Many peroxisomal matrix proteins are imported as
a. folded proteins
b. nascent chains in the process of completing their elongation
c. protein fragments that are spliced together within the peroxisome
d. unfolded proteins

10. Tom is an abbreviation for _____________________________________________________.

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