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Journal of Cell Science, Vol 113, Issue 13 2331-2343, Copyright © 2000 by Company of Biologists

JOURNAL ARTICLES

Spectrin tethers and mesh in the biosynthetic pathway

MA De Matteis and JS Morrow
Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, Santa Maria Imbaro (Chieti), Italy. demattei@cmns.mnegri.it

The paradox of how the Golgi and other organelles can sort a continuous flux of protein and lipid but maintain temporal and morphological stability remains unresolved. Recent discoveries highlight a role for the cytoskeleton in guiding the structure and dynamics of organelles. Perhaps one of the more striking, albeit less expected, of these discoveries is the recognition that a spectrin skeleton associates with many organelles and contributes to the maintenance of Golgi structure and the efficiency of protein trafficking in the early secretory pathway. Spectrin interacts directly with phosphoinositides and with membrane proteins. The small GTPase ARF, a key player in Golgi dynamics, regulates the assembly of the Golgi spectrin skeleton through its ability to control phosphoinositide levels in Golgi membranes, whereas adapter molecules such as ankyrin link spectrin to other membrane proteins. Direct interactions of spectrin with actin and centractin (ARP1) provide a link to dynein, myosin and presumably other motors involved with intracellular transport. Building on the recognized ability of spectrin to organize macromolecular complexes of membrane and cytosolic proteins into a multifaceted scaffold linked to filamentous structural elements (termed linked mosaics), recent evidence supports a similar role for spectrin in organelle function and the secretory pathway. Two working models accommodate much of the available data: the Golgi mesh hypothesis and the spectrin ankyrin adapter protein tethering system (SAATS) hypothesis.
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M. Braun
Association of Spectrin-Like Proteins with the Actin-Organized Aggregate of Endoplasmic Reticulum in the Spitzenkorper of Gravitropically Tip-Growing Plant Cells
Plant Physiology, April 1, 2001; 125(4): 1611 - 1619.
[Abstract] [Full Text]

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 DevelopmentHome page
E. Liao, B. Paw, L. Peters, A Zapata, S. Pratt, C. Do, G Lieschke, and L. Zon
Hereditary spherocytosis in zebrafish riesling illustrates evolution of erythroid beta-spectrin structure, and function in red cell morphogenesis and membrane stability
Development, January 12, 2000; 127(23): 5123 - 5132.
[Abstract] [PDF]

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 J. Biol. Chem.Home page
P. R. Stabach and J. S. Morrow
Identification and Characterization of beta V Spectrin, a Mammalian Ortholog of Drosophilabeta H Spectrin
J. Biol. Chem., July 7, 2000; 275(28): 21385 - 21395.
[Abstract] [Full Text] [PDF]

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 J. Biol. Chem.Home page
D. Pradhan, C. R. Lombardo, S. Roe, D. L. Rimm, and J. S. Morrow
alpha -Catenin Binds Directly to Spectrin and Facilitates Spectrin-Membrane Assembly in Vivo
J. Biol. Chem., February 2, 2001; 276(6): 4175 - 4181.
[Abstract] [Full Text] [PDF]

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 J. Biol. Chem.Home page
W. T. Tse, J. Tang, O. Jin, C. Korsgren, K. M. John, A. L. Kung, B. Gwynn, L. L. Peters, and S. E. Lux
A New Spectrin, beta IV, Has a Major Truncated Isoform That Associates with Promyelocytic Leukemia Protein Nuclear Bodies and the Nuclear Matrix
J. Biol. Chem., June 22, 2001; 276(26): 23974 - 23985.
[Abstract] [Full Text] [PDF]

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 JCBHome page
M. Komada and P. Soriano
{beta}IV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier
J. Cell Biol., January 21, 2002; 156(2): 337 - 348.
[Abstract] [Full Text] [PDF]

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 JCBHome page
F. Perez, K. Pernet-Gallay, C. Nizak, H. V. Goodson, T. E. Kreis, and B. Goud
CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family
J. Cell Biol., February 18, 2002; 156(4): 631 - 642.
[Abstract] [Full Text] [PDF]

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 Mol. Biol. CellHome page
R. V. Fucini, J.-L. Chen, C. Sharma, M. M. Kessels, and M. Stamnes
Golgi Vesicle Proteins Are Linked to the Assembly of an Actin Complex Defined by mAbp1
Mol. Biol. Cell, February 1, 2002; 13(2): 621 - 631.
[Abstract] [Full Text] [PDF]


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