The Resource The role of the yeast GRD20 protein in membrane trafficking and actin organization, by Robert G. Spelbrink

The role of the yeast GRD20 protein in membrane trafficking and actin organization, by Robert G. Spelbrink

Label
The role of the yeast GRD20 protein in membrane trafficking and actin organization
Title
The role of the yeast GRD20 protein in membrane trafficking and actin organization
Statement of responsibility
by Robert G. Spelbrink
Creator
Subject
Language
eng
Summary
The proper localization of resident membrane proteins to the trans -Golgi network (TGN) involves mechanisms for both TGN retention and retrieval from post-TGN compartments. In this study, we report the identification of a new gene, GRD20 , involved in protein sorting in the TGN/endosomal system of Saccharomyces cerevisiae . A strain carrying a transposon insertion allele of GRD20 exhibited rapid vacuolar degradation of the resident TGN endoprotease Kex2p and aberrantly secreted {u223C}50% of the soluble vacuolar hydrolase carboxypeptidase Y (CPY). The Kex2p mislocalization and CPY missorting phenotypes were exhibited rapidly after loss of Grd20p function in grd20 temperature-sensitive mutant strains indicating that Grd20p plays a direct role in these processes. Surprisingly, little if any vacuolar degradation was observed for the TGN membrane proteins A-ALP and Vps10p, underscoring a difference in trafficking patterns for these proteins compared to that of Kex2p. In addition to TGN membrane protein localization, Grd20p was found to be necessary for proper localization of Och1p, a cis -Golgi mannosyltransferase. The mislocalization of Och1p may be responsible for a glycosylation defect observed in invertase and CPY in grd20 mutants. A grd20 null mutant strain exhibited extremely slow growth and a defect in polarization of the actin cytoskeleton and these two phenotypes were invariably linked in a collection of randomly mutagenized grd20 alleles. Analysis of a collection of grd20 temperature-sensitive strains, all of which were defective for TGN protein sorting, indicated that about half had severe growth and actin defects. In contrast, the other half had modest growth defects and near normal actin polarization. The two classes of mutants indicate that Grd20p contains multiple domains assigned to distinct functions. GRD20 encodes a {u223C}100 kDa hydrophilic protein that exhibits a punctate staining pattern by fluorescence microscopy. A subset of the Grd20p-containing structures was shown to also stain for A-ALP, thus a pool of Grd20p associates with the TGN. By subcellular fractionation, Grd20p was found in both a cytosolic fraction and a membrane-associated fraction. Sedimentation of Grd20p at high speed is not affected by detergent but is affected by salt and EDTA suggesting possible interaction with the cytoskeleton or a large protein complex. The discovery of GRD20 provides strong evidence for a link between the actin cytoskeleton and the mechanism of protein localization to the TGN
Additional physical form
Also available on the Internet.
Cataloging source
MUU
http://library.link/vocab/creatorDate
1970-
http://library.link/vocab/creatorName
Spelbrink, Robert G.
Degree
Ph. D.
Dissertation year
2000.
Government publication
government publication of a state province territory dependency etc
Granting institution
University of Missouri-Columbia
Illustrations
  • illustrations
  • photographs
Index
no index present
Literary form
non fiction
Nature of contents
  • bibliography
  • theses
http://library.link/vocab/subjectName
  • Proteins
  • Biological transport
  • Golgi apparatus
  • Endoplasmic reticulum
  • Cell membranes
  • Yeast
Target audience
specialized
Label
The role of the yeast GRD20 protein in membrane trafficking and actin organization, by Robert G. Spelbrink
Instantiates
Publication
Note
  • Typescript
  • Vita
Bibliography note
Includes bibliographical references (leaves 130-155)
Carrier category
online resource
Carrier category code
cr
Carrier MARC source
rdacarrier
Color
not applicable
Content category
text
Content type code
txt
Content type MARC source
rdacontent
Control code
46726504
Dimensions
29 cm
Extent
xi, 156 leaves
Media category
computer
Media MARC source
rdamedia
Media type code
c
Other physical details
illustrations, color photographs
Specific material designation
remote
Label
The role of the yeast GRD20 protein in membrane trafficking and actin organization, by Robert G. Spelbrink
Publication
Note
  • Typescript
  • Vita
Bibliography note
Includes bibliographical references (leaves 130-155)
Carrier category
online resource
Carrier category code
cr
Carrier MARC source
rdacarrier
Color
not applicable
Content category
text
Content type code
txt
Content type MARC source
rdacontent
Control code
46726504
Dimensions
29 cm
Extent
xi, 156 leaves
Media category
computer
Media MARC source
rdamedia
Media type code
c
Other physical details
illustrations, color photographs
Specific material designation
remote

Library Locations

    • University of Missouri Libraries DepositoryBorrow it
      2908 Lemone Blvd, Columbia, MO, 65211, US
      38.919360 -92.291620
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