Tuesday, July 26, 2011

Forthcoming Peroxisome meetings 2011


July 31 – August 2, 2011
Omaha, Nebraska

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In Sex, Life, Development and Disease
August 7-12, 2011
University of New England
Biddeford, ME

8 August 2011, Monday  
9:10 am - 9:40 am                                                                   
Randy Schekman (UC Berkeley, USA)
"Mechanism of Sorting and Traffic of Peroxisomal Proteins from the ER"

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satellite meeting to Plant Biology 2011
August 11, 2011
Hilton Minneapolis, Minneapolis, Minnesota, USA
17 talks, 21 posters and 42 registered researchers..
online registration is available till 11 August 2011 
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FEBS workshop 2011
from algae to higher plants

PrimoŇ°ten, Croatia
31 August - 3 September 2011

Peroxisome related talks -
31 August  - Wednesday

12:00 –12:15
OEF18 is a novel calcium binding protein at peroxisomes and chloroplasts

14:00 –14:15
The PEX11 family: Deciphering a key player of peroxisomal proliferation

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Saturday 10 September, 10:00 to 17:15
Part of the Special Interest symposia during EMBO meeting 2011 Vienna, Austria.
Organisation: Ida van der Klei, Marten Veenhuis
12 talks by European peroxisome researchers.
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6-10 November 2011
Kumamoto, Japan

09 November 2011
09:00 - 09:30
Ralf Erdmann (Ruhr-Univ. Bochum, Germany)
Functional role of the yeast AAA-peroxins Pex1p and Pex6p in peroxisome biogenesis      
09:30 - 10:00
Yukio Fujiki (Kyushu Univ, Japan)
To be announced
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Sunday, July 24, 2011

New player in ER-Peroxisome field


Peroxisomes proliferate by growth and division as well as they can arise de novo from Endoplasmic reticulum. In yeast, it was recently shown that most PMPs transit to peroxisomes via ER. In mammalian cells, Pex16 and Pex3 are known to target peroxisomes via ER. But the key players involved in this ER-peroxisome transport are still poorly known.

The new study published in PNAS identifies Sec16B as factor essential for Pex16 export from ER to peroxisomes. 
Yonekawa et al, Online published before print on 18 july 2011, PNAS

Sec16B(Sec16S) is a vertebrate specific isoform which is less extensively studied than the Sec61A(Sec16L). Comparing the sizes, Sec16B is almost half the size that of Sec16A and these proteins are able to form heteromeric complexes too.

This study found that, overexpression of Sec16B results in reduced number of peroxisomes and ER localization of Pex16 and Pex3. On the other hand, siRNA mediated knockdown of Sec16B results in tubulated peroxisomes, ER localization of pex16 and degradation of Pex3 by Ubiquitin proteasomal system. Authors also characterized different regions of Sec16B and found that C-terminal of Sec16B which differs from Sec16A, is required for its function in peroxisome biogenesis. Peroxisome vesicle formation from ER is known to be independent of COPII vesicle budding. Sec16A as well as Sec16B are involved formation of COPII vesicles and are targeted to ERES(ER Exit Sites). Authors meticulously shown that, stretch of Sec16B  responsible for its recruitment to ERES is not required for its peroxisome related function.

Further reading

PNAS, May 2011

PNAS, December 2011

BBA Mol Cell Research, in press