Directed movements of ciliary and flagellar membrane components: A review

Bloodgood, Robert A.

doi:10.1016/0248-4900(92)90431-y

Cited by 41 publications

(23 citation statements)

References 76 publications

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“…It is well established that, although the membrane of the primary cilium is continuous with the plasma membrane of the cell, it is a separate membrane domain with a unique complement of proteins (Bloodgood 1992). Numerous previous studies have shown the localization of specific receptors to the primary cilium in a variety of different cell types.…”

Section: The Journal Of Histochemistry and Cytochemistrymentioning

confidence: 99%

Localization of Extracellular Matrix Receptors on the Chondrocyte Primary Cilium

McGlashan

Jensen

Poole

2006

J Histochem Cytochem.

163

146

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(CAP) S U M M A R Y A single primary cilium is found in chondrocytes and other connective tissue cells. We have previously shown that extracellular matrix (ECM) macromolecules such as collagen fibers closely associate with chondrocyte primary cilia, and their points of contact are characterized by electron-opaque plaques suggesting a direct link between the ECM and the cilium. This study examines the expression of receptors for ECM molecules on chondrocyte primary cilia. Embryonic chick sterna were fluorescently labeled with antibodies against a and b integrins, NG2, CD44, and annexin V. Primary cilia were labeled using acetylated a-tubulin antibody. Expression of ECM receptors was examined on chondrocyte plasma membranes and their primary cilia using immunofluorescence and confocal microscopy. All receptors examined showed a punctate distribution on the plasma membrane. a2, a3, and b1 integrins and NG2 were also present on primary cilia, whereas annexin V and CD44 were excluded. The number of receptor-positive cilia varied from 8/50 for NG2 to 43/50 for b1 integrin. This is the first study to demonstrate the expression of integrins and NG2 on chondrocyte primary cilia. The data strongly suggest that chondrocyte primary cilia have the necessary machinery to act as mechanosensors, linking the ECM to cytoplasmic organelles responsible for matrix production and secretion.

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Section: The Journal Of Histochemistry and Cytochemistrymentioning

confidence: 99%

Localization of Extracellular Matrix Receptors on the Chondrocyte Primary Cilium

McGlashan

Jensen

Poole

2006

J Histochem Cytochem.

163

146

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“…There is compelling evidence that intraflagellar transport is responsible for carrying flagellar precursors into newly forming flagella and for returning flagellar components to the cytoplasm during flagellar resorption. It is likely that this system also is involved in the constitutive turnover of flagellar components in intact cilia/flagella (78,(81)(82)(83)(84), although other motility mechanisms also may play a role (6,13,85).…”

Section: Regulated Translocation Of a Protein Into An Intactmentioning

confidence: 99%

Regulated Targeting of a Protein Kinase into an Intact Flagellum

Pan

Snell

2000

Journal of Biological Chemistry

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In the green alga Chlamydomonas reinhardtii flagellar adhesion between gametes of opposite mating types leads to rapid cellular changes, events collectively termed gamete activation, that prepare the gametes for cell-cell fusion. As is true for gametes of most organisms, the cellular and molecular mechanisms that underlie gamete activation are poorly understood. Here we report on the regulated movement of a newly identified protein kinase, Chlamydomonas aurora/Ipl1p-like protein kinase (CALK), from the cell body to the flagella during gamete activation. CALK encodes a protein of 769 amino acids and is the newest member of the aurora/ Ipl1p protein kinase family. Immunoblotting with an anti-CALK antibody showed that CALK was present as a 78/80-kDa doublet in vegetative cells and unactivated gametes of both mating types and was localized primarily in cell bodies. In cells undergoing fertilization, the 78-kDa CALK was rapidly targeted to the flagella, and within 5 min after mixing gametes of opposite mating types, the level of CALK in the flagella began to approach levels normally found in the cell body. Protein synthesis was not required for targeting, indicating that the translocated CALK and the cellular molecules required for its movement are present in unactivated gametes. CALK was also translocated to the flagella during flagellar adhesion of nonfusing mutant gametes, demonstrating that cell fusion was not required for movement. Finally, the requirement for flagellar adhesion could be bypassed; incubation of cells of a single mating type in dibutyryl cAMP led to CALK translocation to flagella in gametes but not vegetative cells. These experiments document a new event in gamete activation in Chlamydomonas and reveal the existence of a mechanism for regulated translocation of molecules into an intact flagellum.Cell-cell interactions leading to fusion between gametes of opposite sexes during fertilization are complex processes that involve dramatic changes in each of the interacting gametes. In most multicellular organisms, interactions between adhesion molecules/receptors on the sperm plasma membrane and ligands on the egg surface activate poorly understood signaling pathways that bring about transformation of the sperm into a fusion competent, activated gamete (1). For example, the sperm surface is remodeled as a consequence of the acrosome reaction, an event that accompanies gamete activation, and previously existing adhesion molecules are mobilized to new sites on the sperm (2-4). The molecular mechanisms that underlie and regulate signal transduction and movement of molecules between different gamete compartments during gamete activation largely are unknown (2).As in multicellular organisms, gamete activation and fertilization in the unicellular green alga Chlamydomonas (5) depend on adhesion-induced signaling pathways and intercompartmental communication. At the completion of gametogenesis, during which asexually growing mtϩ and mtϪ vegetative cells differentiate into sexually competent cells, the resultin...

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“…Surface motility in Chlamydomonas cells includes gliding along substrates using flagellar membrane adherence, flagella-flagella contact between two cells during mating, and surface motility observed using polystyrene beads adhered to the flagellar membrane (for a review, see Bloodgood, 1992b). Flagellar surface motility is predicted to involve a microtubulebased motor protein associated with the flagellar membrane and linked to flagellar glycoproteins that adhere to a surface.…”

Section: A Fraction Of Crkcbp Localizes To Flagellamentioning

confidence: 99%

A kinesin-like calmodulin-binding protein inChlamydomonas: evidence for a role in cell division and flagellar functions

Dymek

Goduti

Kramer

et al. 2006

Journal of Cell Science

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Kinesin-like calmodulin-binding protein, KCBP, is a novel member of the C-kinesin superfamily first discovered in flowering plants. This minus-end-directed kinesin exhibits Ca2+-calmodulin-sensitive motor activity in vitro and has been implicated in trichome morphogenesis and cell division. A homologue of KCBP is also found in the unicellular, biflagellate green alga Chlamydomonas reinhardtii (CrKCBP). Unlike plant cells, Chlamydomonas cells do not form trichomes and do not assemble a phragmoplast before cell division. To test whether CrKCBP is involved in additional microtubule-based processes not observed in plants, we generated antibodies against the putative calmodulin-binding domain and used these antibodies in biochemical and localization studies. In interphase cells CrKCBP primarily localizes near the base of the flagella, although surprisingly, a small fraction also localizes along the length of the flagella. CrKCBP is bound to isolated axonemes in an ATP-dependent fashion and is not a component of the dynein arms, radial spokes or central apparatus. During mitosis, CrKCBP appears concentrated at the centrosomes during prophase and metaphase. However, during telophase and cytokinesis CrKCBP co-localizes with the microtubules associated with the phycoplast. These studies implicate CrKCBP in flagellar functions as well as cell division.

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Directed movements of ciliary and flagellar membrane components: A review

Cited by 41 publications

References 76 publications

Localization of Extracellular Matrix Receptors on the Chondrocyte Primary Cilium

Localization of Extracellular Matrix Receptors on the Chondrocyte Primary Cilium

Regulated Targeting of a Protein Kinase into an Intact Flagellum

A kinesin-like calmodulin-binding protein inChlamydomonas: evidence for a role in cell division and flagellar functions

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