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Title 

Implication of mouse Vps26b-Vps29-Vps35 retromer complex in sortilin trafficking

 

솔트린 수송에 관여하는 리트로머 분자

Authors 

Ekyune KimYoung Jeon LeeH J LeeJi Su KimBong Seok SongJae Won HuhSang Rae LeeSun-Uk KimKim Sang-HyunY HongI ShimKyu Tae Chang

Publisher 

Elsevier

Issue Date 

2010

Citation 

Biochemical and Biophysical Research Communications, vol. 403, no. 2, pp. 167-171

Keywords 

The retromer complex, which mediates retrograde transport from endosomes to the trans-Golgi network, is a heteropentameric complex that contains a multifunctional cargo recognition heterotrimer consisted of the vacuolar protein sorting (Vps) subunits Vps26, Vps29, and Vps35. In mammals, there are two different isoforms of Vps26, Vps26a and Vps26b, that localize to the endosome, and to the plasma membrane, respectively. To elucidate the biological significance of the Vps26b isoform, we generated Vps26b knockout mice and studied their molecular, histological, and behavioral phenotypes. We found that the loss of Vps26b results in no significant defects in the behavior, body size, and health of the mice. Vps26b-deficient mice showed a severe reduction of Vps35 protein at cellular level and lacked the Vps26b-Vps29-Vps35 retromer complex, despite the normal presence of the Vps26a-Vps29-Vps35 retromer complex. Relatively, the amount of sortilin was increased approximately 20% in the Vps26b-deficient mice, whereas the sorLA was normal. These results suggest that mouse Vps26b-Vps29-Vps35 retromer complex is implicated in the transport of sortilin from endosomes to the trans-Golgi network (TGN).

Abstract 

Endosomes; Retromer complex; Trans-Golgi network (TGN); Vacuolar protein sorting 26b (Vps26b); Vps26b-deficient mice

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2010.10.121

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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