Match the protein on the left with the mechanism of how the protein is activated on the right. Beclin-1 XBP-15 Rheb LC3 IRE-1 [Choose] [Choose] Phosphorylation Binding another protein to form a complex Dephosphorylation Cleavage Binding of GTP Dimerization Splicing in cytoplasm [Choose] [Choose]

Match the protein on the left with the mechanism of how the protein is activated on the right. Beclin-1 XBP-15 Rheb LC3 IRE-1 [Choose] [Choose] Phosphorylation Binding another protein to form a complex Dephosphorylation Cleavage Binding of GTP Dimerization Splicing in cytoplasm [Choose] [Choose]

Name: Match the protein on the left with the mechanism of how the protein i
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Description: Match the protein on the left with the mechanism of how the protein is activated on the right.Beclin-1XBP-1sRhebLC3IRE-1[Choose][Choose]PhosphorylationBinding another protein to form a complexDephosphorylationCleavageBinding of GTPDimerizationSplici

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter9: Cell Communication

Section: Chapter Questions

Problem 1VCQ: Figure 9.8 HER2 is a receptor tyrosine kinase. In 30 percent of human breast cancers, HER2 is...

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Match the protein on the left with the type of activation of that protein on the right STAT Smad PKA Ras NFKB Nuclear receptor [Choose] [Choose] GTP binding serine phosphorylation Interaction with Galpha Cleavage by y-secretase destruction of a protein by proteasome tyrosine phosphorylation second messenger ligand binding [Choose] [Choose] [Choose]
Which describes an enzymatic activity/biochemical function of importin-beta? facilitate release of nuclear proteins after transport through the nuclear pore complex interact with/bind to nuclear localization sequences INLSS) interact with/bind to importin-alpha hydrolyze GTP to GDP + Pi
The affinity of integrins for matrix components canbe modulated by changes to their cytoplasmic domains:a process known as inside-out signaling. You have iden-tified a key region in the cytoplasmic domains of αIIbβ3integrin that seems to be required for inside-out signaling(Figure Q19–3). Substitution of alanine for either D723in the β chain or R995 in the α chain leads to a high levelof spontaneous activation, under conditions where thewild-type chains are inactive. Your advisor suggests thatyou convert the aspartate in the β chain to an arginine(D723R) and the arginine in the α chain to an aspartate(R995D). You compare all three α chains (R995, R995A,and R995D) against all three β chains (D723, D723A, andD723R). You find that all pairs have a high level of sponta-neous activation, except D723 vs R995 (the wild type) andD723R vs R995D, which have low levels. Based on theseresults, how do you think the αIIbβ3 integrin is held in itsinactive state?
Predict the location(s) (intracellular or extracelular) and a brief description of WHY based on your knowledge of the transport processes in the following constructs. Assume a start codon is present and include any proteolytic processing that would be likely. 1. A PTS1 C-term peroxisomal targeting seq added to C term of a normally secreted protein with usual N -terminal signal sequence 2. Adding of N-terminal mitochondrial targeting sequence to protein with internal nuclear localization seq. 3. Adding N-terminal signal sequence of secreted protein to N-terminus a mitochondria matrix protein precursor with mitochondrial targeting sequence still present
Match the primary sequence to its characteristics/function/fate N-signal signal-anchor stop-anchor nuclear localization sequence KDEL 1. found at carboxyl terminus of ER resident proteins, interaction with its receptor directs retrieval from Golgi 2. hydrophobic, interacts with SRP and translocon, becomes transmembrane helix 3. mostly hydrophobic, interacts with SRP, cut off 4. hydrophobic, interacts with translocon, becomes transmembrane helix 5. basic, interacts with importin-alpha
TGF-B Receptor I (RI) phosphorylation of Smad2/3 does all of the following EXCEPT: activate Smad2/3 binding to the Co-Smad Smad4 dissociate intramolecular binding of Smad2/3 MH1 and MH2 domains. RI phosphorylation of Smad2/3 does all of these things. release Smad2/3 from the nucleus into the cytoplasm unmask the Smad2/3 nuclear localization signal (NLS).
What would most likely occur to nuclear-cytoplasmic shuttling if the intrinsic GTPase activity of RAN was slowed down by 50%? Group of answer choices RAN would not bind exportin and proteins would accumulate in the nucleus All of the answers are likely None of the answers are likely Importin beta would not release from RAN in the cytoplasm and nuclear import would slow down RAN would not bind to importin beta and protein cargo in the nucleus would not release
15.3 Explain the fellovine diaeram: prospective nuclear protein nuclear Ran HYDROLYZES ITS BOUND GTP, localization Ran-GDP ignal Ran-GDP DISSOCIATES PROTEIN BINDS FROM RECEPTOR TO RECEPTOR nuclear pore CYTOSOL NUCLEUS Ran-GTP BINDS PROTEIN DELIVERED TO NUCLEUS TO RECEPTOR Ran-GTP 15.4 EXplain the followine.diBEram: SRP displaced and released for reuse MRNA ribosome signal- recognition particle (SRP) CYTOSOL growing- polypeptide chain ER signal sequence ER LUMEN SRP receptor protein translocator Ngam 1514 Iereoog ed.arinde 15.5 Explain the following.diaeram: newly synthesized soluble proteins for constitutive newly synthesized plasma membrane lipids transport vesicde secretion CONSTITUTIVE SECRETION unregulated exocytosis plasma membrane newly synthesized plasma membrane protein extracellular signal such as trans Golgi network homone or neurotransmitter signal transduction REGULATED SECRETION regulated екосуtosis secretory vesicle storing secretory proteins Golgi apparatus CYTOSOL…
Microtubules in an animal cell: O a. undergo assembly if the concentration of GTP-bound tubulin dimers is high and a cell is exposed to vinblastine O b. undergo disassembly if the concentration of GDP-bound tubulin dimers is high and a cell is exposed to taxol O c. undergo disassembly if the concentration of GTP-bound tubulin dimers is high and a cell is exposed to colchicine O d. undergo assembly if the concentration of GTP-bound tubulin dimers is high and a cell is exposed to colchicine
Figure 9.8 HER2 is a receptor tyrosine kinase. In 30 percent of human breast cancers, HER2 is permanently activated, resulting in unregulated cell division. Lapatinib, a drug used to treat breast cancer, inhibits HER2 receptor tyrosine kinase autophosphorylation (the process by which the receptor adds phosphates onto itself), thus reducing tumor growth by 50 percent. Besides autophosphorylation, which of the following steps would be inhibited by Lapatinib? Signaling molecule binding, dimerization, and the downstream cellular response. Dimerization, and the downstream cellular response. The downstream cellular response. Phosphatase activity, dimerization, and the downsteam cellular response.
What is the best inhibitor of endoplasmic reticulum stress in human ?
Indicate (x) if the following statements about synthesis of proteins containing an ER signal sequence are True or False: True False i. Translation is initiated by ribosomes located on the ER membrane The signal recognition particle (SRP) binds a sequence of nonpolar (hydrophobic) amino acids. ii. iii. The ER signal sequence may be cleaved by signal peptidase on the cytoplasmic side of the ER membrane. iv. The part of a transmembrane protein that will ultimately be located outside of the cell is inserted into the lumen of the ER during translation. A stop transfer sequence is a series of polar amino acids that halts translocation of a newly synthesized peptide into the ER lumen.