scholarly journals Evidence for the Involvement of Kif4 in the Anterograde Transport of L1-Containing Vesicles

2000 ◽  
Vol 149 (1) ◽  
pp. 141-152 ◽  
Author(s):  
Diego Peretti ◽  
Leticia Peris ◽  
Silvana Rosso ◽  
Santiago Quiroga ◽  
Alfredo Cáceres
Keyword(s):  
Growth Cone ◽  
Antisense Oligonucleotides ◽  
Cell Adhesion Molecule ◽  
Neuronal Development ◽  
Subcellular Fractionation ◽  
Complete Disappearance ◽  
Cellular Functions ◽  
Anterograde Transport ◽  
Axonal Elongation ◽  
A Cell

In this study we present evidence about the cellular functions of KIF4. Using subcellular fractionation techniques and immunoisolation, we have now identified a type of vesicle that associates with KIF4, an NH2-terminal globular motor domain kinesin-like protein. This vesicle is highly concentrated in growth cones and contains L1, a cell adhesion molecule implicated in axonal elongation. It lacks synaptic vesicle markers, receptors for neurotrophins, and membrane proteins involved in growth cone guidance. In cultured neurons, KIF4 and L1 predominantly localize to the axonal shaft and its growth cone. Suppression of KIF4 with antisense oligonucleotides results in the accumulation of L1 within the cell body and in its complete disappearance from axonal tips. In addition, KIF4 suppression prevents L1-enhanced axonal elongation. Taken collectively, our results suggest an important role for KIF4 during neuronal development, a phenomenon which may be related to the anterograde transport of L1-containing vesicles.

scholarly journals Suppression of KIF2 in PC12 Cells Alters the Distribution of a Growth Cone Nonsynaptic Membrane Receptor and Inhibits Neurite Extension

1997 ◽  
Vol 138 (3) ◽  
pp. 657-669 ◽  
Author(s):  
Gerardo Morfini ◽  
Santiago Quiroga ◽  
Alberto Rosa ◽  
Kenneth Kosik ◽  
Alfredo Cáceres
Keyword(s):  
Pc12 Cells ◽  
Nerve Cell ◽  
Growth Cone ◽  
Growth Cones ◽  
Subcellular Fractionation ◽  
Membrane Receptor ◽  
Complete Disappearance ◽  
Anterograde Transport ◽  
Neurite Extension ◽  
Developing Neurons

In the present study, we present evidence about the cellular functions of KIF2, a kinesin-like superfamily member having a unique structure in that its motor domain is localized at the center of the molecule (Noda Y., Y. Sato-Yoshitake, S. Kondo, M. Nangaku, and N. Hirokawa. 1995. J. Cell Biol. 129:157–167.). Using subcellular fractionation techniques, isopicnic sucrose density centrifugation of microsomal fractions from developing rat cerebral cortex, and immunoisolation with KIF2 antibodies, we have now identified a type of nonsynaptic vesicle that associates with KIF2. This type of organelle lacks synaptic vesicle markers (synapsin, synaptophysin), amyloid precursor protein, GAP-43, or N-cadherin. On the other hand, it contains βgc, which is a novel variant of the β subunit of the IGF-1 receptor, which is highly enriched in growth cone membranes. Both βgc and KIF2 are upregulated by NGF in PC12 cells and highly concentrated in growth cones of developing neurons. We have also analyzed the consequences of KIF2 suppression by antisense oligonucleotide treatment on nerve cell morphogenesis and the distribution of synaptic and nonsynaptic vesicle markers. KIF2 suppression results in a dramatic accumulation of βgc within the cell body and in its complete disappearance from growth cones; no alterations in the distribution of synapsin, synaptophysin, GAP-43, or amyloid percursor protein are detected in KIF2-suppressed neurons. Instead, all of them remained highly enriched at nerve terminals. KIF2 suppression also produces a dramatic inhibition of neurite outgrowth; this phenomenon occurs after βgc has disappeared from growth cones. Taken collectively, our results suggest an important role for KIF2 in neurite extension, a phenomenon that may be related with the anterograde transport of a type of nonsynaptic vesicle that contains as one of its components a growth cone membrane receptor for IGF-1, a growth factor implicated in nerve cell development.

Function and Histopathology of a Cell Adhesion Molecule TSLC1 in Cancer

2011 ◽  
Vol 29 (2) ◽  
pp. 107-112 ◽  
Author(s):  
Qi-Lian Liang ◽  
Guo-Qiang Chen ◽  
Zhou-Yu Li ◽  
Bi-Rong Wang
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
A Cell

Sterol and lipid trafficking in mammalian cells

2006 ◽  
Vol 34 (3) ◽  
pp. 335-339 ◽  
Author(s):  
F.R. Maxfield ◽  
M. Mondal
Keyword(s):  
Membrane Trafficking ◽  
Mammalian Cells ◽  
Intracellular Transport ◽  
Vesicular Transport ◽  
Cholesterol Content ◽  
Cellular Functions ◽  
Lipid Trafficking ◽  
Sterol Transport ◽  
A Cell ◽  
Asymmetrically Distributed

The pathways involved in the intracellular transport and distribution of lipids in general, and sterols in particular, are poorly understood. Cholesterol plays a major role in modulating membrane bilayer structure and important cellular functions, including signal transduction and membrane trafficking. Both the overall cholesterol content of a cell, as well as its distribution in specific organellar membranes are stringently regulated. Several diseases, many of which are incurable at present, have been characterized as results of impaired cholesterol transport and/or storage in the cells. Despite their importance, many fundamental aspects of intracellular sterol transport and distribution are not well understood. For instance, the relative roles of vesicular and non-vesicular transport of cholesterol have not yet been fully determined, nor are the non-vesicular transport mechanisms well characterized. Similarly, whether cholesterol is asymmetrically distributed between the two leaflets of biological membranes, and if so, how this asymmetry is maintained, is poorly understood. In this review, we present a summary of the current understanding of these aspects of intracellular trafficking and distribution of lipids, and more specifically, of sterols.

Design of a Calcium-Binding Protein with Desired Structure in a Cell Adhesion Molecule

2005 ◽  
Vol 127 (7) ◽  
pp. 2085-2093 ◽  
Author(s):  
Wei Yang ◽  
Anna L. Wilkins ◽  
Yiming Ye ◽  
Zhi-ren Liu ◽  
Shun-yi Li ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Adhesion Molecule ◽  
Calcium Binding ◽  
Cell Adhesion Molecule ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
A Cell

scholarly journals Molecular regulation of GLUT-4 targeting in 3T3-L1 adipocytes.

1995 ◽  
Vol 130 (5) ◽  
pp. 1081-1091 ◽  
Author(s):  
B J Marsh ◽  
R A Alm ◽  
S R McIntosh ◽  
D E James
Keyword(s):  
Cell Surface ◽  
Glucose Transporter ◽  
Subcellular Fractionation ◽  
Molecular Regulation ◽  
Surface Distribution ◽  
Amino Terminal ◽  
Glut 4 ◽  
Dileucine Motif ◽  
A Cell ◽  
Insulin Dependent

Insulin stimulates glucose transport in muscle and adipose tissue by triggering the movement of the glucose transporter GLUT-4 from an intracellular compartment to the cell surface. Fundamental to this process is the intracellular sequestration of GLUT-4 in nonstimulated cells. Two distinct targeting motifs in the amino and carboxy termini of GLUT-4 have been previously identified by expressing chimeras comprised of portions of GLUT-4 and GLUT-1, a transporter isoform that is constitutively targeted to the cell surface, in heterologous cells. These motifs-FQQI in the NH2 terminus and LL in the COOH terminus-resemble endocytic signals that have been described in other proteins. In the present study we have investigated the roles of these motifs in GLUT-4 targeting in insulin-sensitive cells. Epitope-tagged GLUT-4 constructs engineered to differentiate between endogenous and transfected GLUT-4 were stably expressed in 3T3-L1 adipocytes. Targeting was assessed in cells incubated in the presence or absence of insulin by subcellular fractionation. The targeting of epitope-tagged GLUT-4 was indistinguishable from endogenous GLUT-4. Mutation of the FQQI motif (F5 to A5) caused GLUT-4 to constitutively accumulate at the cell surface regardless of expression level. Mutation of the dileucine motif (L489L490 to A489A490) caused an increase in cell surface distribution only at higher levels of expression, but the overall cells surface distribution of this mutant was less than that of the amino-terminal mutants. Both NH2- and COOH-terminal mutants retained insulin-dependent movement from an intracellular to a cell surface locale, suggesting that neither of these motifs is involved in the insulin-dependent redistribution of GLUT-4. We conclude that the phenylalanine-based NH2-terminal and the dileucine-based COOH-terminal motifs play important and distinct roles in GLUT-4 targeting in 3T3-L1 adipocytes.

scholarly journals Potential role of SC1, a cell adhesion molecule, in mammary gland tumors

2008 ◽  
Author(s):  
Kenji Hagimori ◽  
Hidenori Kato ◽  
Keiko Fukuda ◽  
Masaharu Kikuta ◽  
Yasuhiro Tsukamoto ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Mammary Gland ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Potential Role ◽  
Mammary Gland Tumors ◽  
A Cell
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