Limits...
Let's make Golgi.

Wells WA - J. Cell Biol. (2001)

Bottom Line: Does the Golgi self-organize or does it form around an instructive template?Evidence on both sides is piling up, but a definitive conclusion is proving elusive.

View Article: PubMed Central - PubMed

Affiliation: wellw@rockefeller.edu

ABSTRACT
Does the Golgi self-organize or does it form around an instructive template? Evidence on both sides is piling up, but a definitive conclusion is proving elusive.

Show MeSH
It takes a higher concentration of dominant Sar1 (in the GTP form) to force a matrix protein out of the Golgi region.
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Related In: Results  -  Collection


getmorefigures.php?uid=PMC2198868&req=5

fig1: It takes a higher concentration of dominant Sar1 (in the GTP form) to force a matrix protein out of the Golgi region.

Mentions: Two papers in this issue contest the matrix interpretation. Brian Storrie (Virginia Tech, Blacksburg, VA) uses a higher concentration of the Sar1 mutant used by Warren (which is stuck in the active, GTP-loaded state) and finds that now both Golgi enzymes and matrix proteins leave the Golgi (see Miles et al. on page 543 and Fig. 1). Lippincott-Schwartz uses an alternative Sar1 mutant, this one stuck in the inactive, GDP-loaded state, to show that Golgi enzymes and matrix proteins can be forced back into the ER (see Ward et al. on page 557 and Fig. 2). In FRAP experiments, Ward et al. also show that Golgi matrix proteins can exchange dynamically rather than acting as a static matrix.


Let's make Golgi.

Wells WA - J. Cell Biol. (2001)

It takes a higher concentration of dominant Sar1 (in the GTP form) to force a matrix protein out of the Golgi region.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2198868&req=5

fig1: It takes a higher concentration of dominant Sar1 (in the GTP form) to force a matrix protein out of the Golgi region.
Mentions: Two papers in this issue contest the matrix interpretation. Brian Storrie (Virginia Tech, Blacksburg, VA) uses a higher concentration of the Sar1 mutant used by Warren (which is stuck in the active, GTP-loaded state) and finds that now both Golgi enzymes and matrix proteins leave the Golgi (see Miles et al. on page 543 and Fig. 1). Lippincott-Schwartz uses an alternative Sar1 mutant, this one stuck in the inactive, GDP-loaded state, to show that Golgi enzymes and matrix proteins can be forced back into the ER (see Ward et al. on page 557 and Fig. 2). In FRAP experiments, Ward et al. also show that Golgi matrix proteins can exchange dynamically rather than acting as a static matrix.

Bottom Line: Does the Golgi self-organize or does it form around an instructive template?Evidence on both sides is piling up, but a definitive conclusion is proving elusive.

View Article: PubMed Central - PubMed

Affiliation: wellw@rockefeller.edu

ABSTRACT
Does the Golgi self-organize or does it form around an instructive template? Evidence on both sides is piling up, but a definitive conclusion is proving elusive.

Show MeSH