CIC-7 requires Ostm1 as a beta-subunit to support bone resorption and lysosomal function
Article Abstract:
A study showing that both CIC-7 and Ostm1 proteins co-localize in late endosomes and lysosomes of various tissues, as well as in the ruffled border of bone-resorbing osteoclasts is illustrated. Co-immunoprecipitations show that CIC-7 and Ostm1 form a molecular complex and suggest that Ostm1 is a beta-subunit of CIC-7 and CIC-7 is required for Ostm1 to reach lysosomes, where the highly glycosylated Ostm1 luminal domain is cleaved.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
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Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins
Article Abstract:
A study was conducted to show that the two mainly endosomal proteins CLC-4 and CLC-5 function as electrogenic chloride/proton exchangers, resembling the transport activity of the bacterial protein ClC-e1. The results demonstrate that chloride/proton exchange activity is not just a peculiarity of a bacterial CLC protein, but rather that a dichotomy between transporters and channels exist within the mammalian CLC family.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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Do neural signals remodel bone?
Article Abstract:
A study conducted by Gerard Karsenty and colleagues show that leptin affects bone mass. He further states that bone renews itself by a process called remodeling, where cells called osteoclasts eat the old bones and cells called osteoblasts lay down new bone.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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