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Review
, 113 (7), 2193-200

Subcellular Dynamics of Multifunctional Protein Regulation: Mechanisms of GAPDH Intracellular Translocation

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Review

Subcellular Dynamics of Multifunctional Protein Regulation: Mechanisms of GAPDH Intracellular Translocation

Michael A Sirover. J Cell Biochem.

Abstract

Multidimensional proteins such as glyceraldehyde-3-phosphate dehydrogenase (GAPDH) exhibit distinct activities unrelated to their originally identified functions. Apart from glycolysis, GAPDH participates in iron metabolism, membrane trafficking, histone biosynthesis, the maintenance of DNA integrity and receptor mediated cell signaling. Further, multifunctional proteins exhibit distinct changes in their subcellular localization reflecting their new activities. As such, GAPDH is not only a cytosolic protein but is localized in the membrane, the nucleus, polysomes, the ER and the Golgi. In addition, although the initial subcellular localizations of multifunctional proteins may be of significance, dynamic changes in intracellular distribution may occur as a consequence of those new activities. As such, regulatory mechanisms may exist through which cells control multifunctional protein expression as a function of their subcellular localization. The temporal sequence through which subcellular translocation and the acquisition of new GAPDH functions is considered as well as post-translational modification as a basis for its intracellular transport.

Figures

Figure I
Figure I. Subcellular GAPDH Dynamics
Figure II
Figure II. Constitutive GAPDH Translocation
Figure III
Figure III. GAPDH and the Maintenance of DNA Integrity
Figure IV
Figure IV. Inducible GAPDH Translocation
Figure V
Figure V. GAPDH and Receptor Mediated Cell Signaling
Figure VI
Figure VI. Semi-Constitutive GAPDH Translocation

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