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Molecular Biology Commons

Open Access. Powered by Scholars. Published by Universities.®

2003

University of Massachusetts Amherst

Articles 1 - 2 of 2

Full-Text Articles in Molecular Biology

Dependence Of Endoplasmic Reticulum-Associated Degradation On The Peptide Binding Domain And Concentration Of Bip, Mehdi Kabani, Stephanie S. Kelley, Michael W. Morrow, Diana L. Montgomery, Renuka Sivendran, Mark D. Rose, Lila Gierasch, Jeffrey L. Brodsky Mar 2003

Dependence Of Endoplasmic Reticulum-Associated Degradation On The Peptide Binding Domain And Concentration Of Bip, Mehdi Kabani, Stephanie S. Kelley, Michael W. Morrow, Diana L. Montgomery, Renuka Sivendran, Mark D. Rose, Lila Gierasch, Jeffrey L. Brodsky

Lila Gierasch

ER-associated degradation (ERAD) removes defective and mis-folded proteins from the eukaryotic secretory pathway, but mutations in the ER lumenal Hsp70, BiP/Kar2p, compromise ERAD efficiency in yeast. Because attenuation of ERAD activates the UPR, we screened for kar2 mutants in which the unfolded protein response (UPR) was induced in order to better define how BiP facilitates ERAD. Among the kar2 mutants isolated we identified the ERAD-specific kar2-1 allele (Brodsky et al. J. Biol. Chem. 274, 3453–3460). The kar2-1 mutation resides in the peptide-binding domain of BiP and decreases BiP's affinity for a peptide substrate. Peptide-stimulated ATPase activity was also reduced, suggesting …


Actin-Depolymerizing Factor Mediates Rac/Rop Gtpase-Regulated Pollen Tube Growth, C, Y, Chen, Alice Cheung, H. M. Wu Jan 2003

Actin-Depolymerizing Factor Mediates Rac/Rop Gtpase-Regulated Pollen Tube Growth, C, Y, Chen, Alice Cheung, H. M. Wu

Alice Cheung

Pollen tube elongation is a rapid tip growth process that is driven by a dynamic actin cytoskeleton. A ubiquitous family of actin binding proteins, actin-depolymerizing factors (ADFs)/cofilins, bind to actin filaments, induce severing, enhance depolymerization from their slow-growing end, and are important for maintaining actin dynamics in vivo. ADFs/cofilins are regulated by multiple mechanisms, among which Rho small GTPase-activated phosphorylation at a terminal region Ser residue plays an important role in regulating their actin binding and depolymerizing activity, affecting actin reorganization. We have shown previously that a tobacco pollen-specific ADF, NtADF1, is important for maintaining normal pollen tube actin cytoskeleton …