Subcellular Localization of Mammalian Type II Membrane Proteins

Aturaliya, Rajith; Fink, J. Lynn; Davis, Melissa J.; Teasdale, Melvena; Hanson, Kelly; Miranda, Kevin C.; Forrest, Alistair R.R.; Grimmond, Sean M.; Suzuki, Harukazu; Kanamori, Mutsumi; Cui, Kai; Kawai, Jun; Carninci, Piero; Hayashizaki, Yoshihide; Teasdale, Rohan D.

doi:10.1111/j.1600-0854.2006.00407.x

Cited by 19 publications

(18 citation statements)

References 49 publications

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“…The short NH 2 -terminal hydrophobic tract found in Aplysia cyclase is longer in CD38, the result of a process simply requiring the addition of a few amino acid residues to produce a type II membrane protein with an NH 2 -terminal transmembrane domain. The fate of most type II proteins is associated with the plasma membrane, Golgi apparatus, and endoplasmic reticulum (ER) (11). This is also the case with CD38, which thus became an ectoenzyme during its long course through evolution.…”

Section: A From One Soluble Gene To a Family Of Transmembrane Proteinsmentioning

confidence: 95%

Evolution and Function of the ADP Ribosyl Cyclase/CD38 Gene Family in Physiology and Pathology

Malavasi¹,

Deaglio²,

Funaro³

et al. 2008

Physiological Reviews

747

794

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The membrane proteins CD38 and CD157 belong to an evolutionarily conserved family of enzymes that play crucial roles in human physiology. Expressed in distinct patterns in most tissues, CD38 (and CD157) cleaves NAD(+) and NADP(+), generating cyclic ADP ribose (cADPR), NAADP, and ADPR. These reaction products are essential for the regulation of intracellular Ca(2+), the most ancient and universal cell signaling system. The entire family of enzymes controls complex processes, including egg fertilization, cell activation and proliferation, muscle contraction, hormone secretion, and immune responses. Over the course of evolution, the molecules have developed the ability to interact laterally and frontally with other surface proteins and have acquired receptor-like features. As detailed in this review, the loss of CD38 function is associated with impaired immune responses, metabolic disturbances, and behavioral modifications in mice. CD38 is a powerful disease marker for human leukemias and myelomas, is directly involved in the pathogenesis and outcome of human immunodeficiency virus infection and chronic lymphocytic leukemia, and controls insulin release and the development of diabetes. Here, the data concerning diseases are examined in view of potential clinical applications in diagnosis, prognosis, and therapy. The concluding remarks try to frame all of the currently available information within a unified working model that takes into account both the enzymatic and receptorial functions of the molecules.

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Section: A From One Soluble Gene To a Family Of Transmembrane Proteinsmentioning

confidence: 95%

Evolution and Function of the ADP Ribosyl Cyclase/CD38 Gene Family in Physiology and Pathology

Malavasi¹,

Deaglio²,

Funaro³

et al. 2008

Physiological Reviews

747

794

View full text Add to dashboard Cite

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“…TEMP was previously demonstrated to localise to the plasma membrane and to intracellular punctate structures using a linear, amino-terminal, myc-tagged expression construct [1]. To determine the nature of the intracellular compartments to which TEMP localises, further co-localisation studies were initially performed with two endosome proteins SNX1 and YFP tagged Rabankyrin-5.…”

Section: Resultsmentioning

confidence: 99%

“…Furthermore, for novel proteins for which a function cannot be inferred based on homology to other characterized proteins it is often one of the first traits investigated. Previously, we have performed several high-throughput subcellular localization projects on subsets of mouse proteins defined as part of the FANTOM project to determine the transcriptional output from the mouse genome [1,2,3]. For many of these proteins it represented the first property of these proteins to be determined and many displayed subcellular distributions of interest.…”

Section: Introductionmentioning

confidence: 99%

“…All of the data captured from these projects was compiled and made publicly available on the LOCATE database [4,5,6]. Here we report the initial characterisation of a novel protein TEMP, a Type III Endosome Membrane Protein that displayed a plasma membrane and intracellular punctate subcellular localisation phenotype in the high throughput subcellular localisation screen [1]. Type III membrane proteins have a single membrane-spanning domain that acts as a reverse signal-anchor which results in the translocation of the amino-terminus across the membrane [7].…”

Section: Introductionmentioning

confidence: 99%

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A Novel Type III Endosome Transmembrane Protein, TEMP

Aturaliya

Kerr

Teasdale

2012

Cells

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As part of a high-throughput subcellular localisation project, the protein encoded by the RIKEN mouse cDNA 2610528J11 was expressed and identified to be associated with both endosomes and the plasma membrane. Based on this, we have assigned the name TEMP for Type III Endosome Membrane Protein. TEMP encodes a short protein of 111 amino acids with a single, alpha-helical transmembrane domain. Experimental analysis of its membrane topology demonstrated it is a Type III membrane protein with the amino-terminus in the lumenal, or extracellular region, and the carboxy-terminus in the cytoplasm. In addition to the plasma membrane TEMP was localized to Rab5 positive early endosomes, Rab5/Rab11 positive recycling endosomes but not Rab7 positive late endosomes. Video microscopy in living cells confirmed TEMP’s plasma membrane localization and identified the intracellular endosome compartments to be tubulovesicular. Overexpression of TEMP resulted in the early/recycling endosomes clustering at the cell periphery that was dependent on the presence of intact microtubules. The cellular function of TEMP cannot be inferred based on bioinformatics comparison, but its cellular distribution between early/recycling endosomes and the plasma membrane suggests a role in membrane transport.

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“…For example, LOCATE [5] is a database of mouse protein subcellular localization, which is based on highthrough chip data and data mining of more than 1700 relational documents. And subcellular localization information of mammalian type transmembrane protein was included in this database [6]. Not long ago, Kislinger et al [7] annotated 4768 mouse protein subcellular localizations on the basis of mass spectrometry, and 3274 annotations were highly reliable.…”

Section: Databases Of Protein Subcellular Lo-calizationmentioning

confidence: 99%

A Research on Bioinformatics Prediction of Protein Subcellular Localization

Fang¹,

Tao²,

Zhang

2009

CBIO

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Protein subcellular localization is one of the key characteristic to understand its biological function. Proteins are transported to specific organelles and suborganelles after they are synthesized. They take part in cell activity and function efficiently when correctly localized. Inaccurate subcellular localization will have great impact on cellular function. Prediction of protein subcellular localization is one of the important areas in protein function research. Now it becomes the hot issue in bioinformatics. In this review paper, the recent progress on bioinformatics research of protein subcellular localization and its prospect are discussed.

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Subcellular Localization of Mammalian Type II Membrane Proteins

Cited by 19 publications

References 49 publications

Evolution and Function of the ADP Ribosyl Cyclase/CD38 Gene Family in Physiology and Pathology

Evolution and Function of the ADP Ribosyl Cyclase/CD38 Gene Family in Physiology and Pathology

A Novel Type III Endosome Transmembrane Protein, TEMP

A Research on Bioinformatics Prediction of Protein Subcellular Localization

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