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The mitochondrial preprotein translocases of the outer membrane (Tom) is a multisubunit protein complex that facilitates the import of nucleus-encoded precursor proteins across the mitochondrial outer membrane (1). The Tom machinery consists of import receptors for the initial binding of cytosolically synthesized preproteins and a general import pore (GIP) for the membrane translocation of various preproteins into the mitochondria (2). The import receptors include Tom20 and Tom22, which form

Ribosomal subunits are synthesized in the nucleus, and mature 40S and 60S subunits are exported stoichiometrically into the cytoplasm. Both 40S and 60S subunits are composed of four RNA species and approximately 80 structurally distinct proteins. Mitochondrial ribosomes consist of a small 28S subunit and a large 39S subunit. Ribosomal proteins have the ability to pass through the nuclear envelope in the native state, making them the largest of the structures accommodated by the nuclear por

The protein encoded by the LAMP2 gene is a member of a family of membrane glycoproteins. This glycoprotein provides selectins with carbohydrate ligands and is thought to play a role in tumor cell metastasis. It may also function in the protection, maintenance, and adhesion of the lysosome. Alternative splicing of the gene produces two known products, LAMP2a and LAMP2b. Isoform LAMP2a is highly expressed in placenta, lung and liver and has low expression in brain and skeletal muscle. The i

This gene was identified based on homology to Pichia pastoris GSA7 and Saccharomyces cerevisiae APG7. In the yeast, the protein appears to be required for fusion of peroxisomal and vacuolar membranes. The protein shows homology to the ATP-binding and catalytic sites of the E1 ubiquitin activating enzymes. [provided by RefSeq, Jan 2009].

RAB proteins are GTPases that regulate vesicular trafficking and reside in specific intracellular compartments. RAB9 has been localized to components of the endocytic/exocytic pathway. It has been implicated in the recycling of membrane receptors, such as the mannose 6-phosphate receptor from early endosomes to the trans Golgi network.