Mastigoneme attachment in Ochromonas

Markey, Donald R.; Bouck, G. Benjamin

doi:10.1016/s0022-5320(77)80077-4

Cited by 31 publications

(7 citation statements)

References 5 publications

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“…Chlamydomonas PKD2 forms linear arrays in cilia The PKD2-mastigoneme complex is physically linked to just two of the nine axonemal DMTs. An organization into two rows and association with the axoneme is also typical for mastigonemes in other protists (Markey and Bouck, 1977). PKD2 could bind directly or indirectly to the DMTs.…”

Section: Discussionmentioning

confidence: 79%

Chlamydomonas PKD2 organizes mastigonemes, hair-like glycoprotein polymers on cilia

Liu

Lou

Wingfield

et al. 2020

Journal of Cell Biology

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Mutations in the channel protein PKD2 cause autosomal dominant polycystic kidney disease, but the function of PKD2 in cilia remains unclear. Here, we show that PKD2 targets and anchors mastigonemes, filamentous polymers of the glycoprotein MST1, to the extracellular surface of Chlamydomonas cilia. PKD2–mastigoneme complexes physically connect to the axonemal doublets 4 and 8, positioning them perpendicular to the plane of ciliary beating. pkd2 mutant cilia lack mastigonemes, and mutant cells swim with reduced velocity, indicating a motility-related function of the PKD2–mastigoneme complex. Association with both the axoneme and extracellular structures supports a mechanosensory role of Chlamydomonas PKD2. We propose that PKD2–mastigoneme arrays, on opposing sides of the cilium, could perceive forces during ciliary beating and transfer these signals to locally regulate the response of the axoneme.

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Section: Discussionmentioning

confidence: 79%

Chlamydomonas PKD2 organizes mastigonemes, hair-like glycoprotein polymers on cilia

Liu

Lou

Wingfield

et al. 2020

Journal of Cell Biology

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“…In general, two distinct types of flagellar surface appendages (mastigonemes) have been identified from a variety of organisms bearing at least one anteriorly directed flagellum. Tubular mastigonemes, characterized the most extensively, are found (a) to be relatively uniform structurally among different organisms but differ in detail from phylum to phylum, (b) to consist of one or more proteins or glycoproteins (3,6,7), (c) to originate within the perinuclear continuum-endoplasmic reticulum-Golgi apparatus compartments (cf reference 4), (d) to be firmly attached to the axoneme microtubules (19) and, (e) to reverse the normal thrust of the flagellum so that the organism is capable of movement in the same direction wave propagation (16). Nontubular mastigonemes may be present on the same flagellum as tubular mastigonemes or present alone on the flagellar surface of many flagellates.…”

mentioning

confidence: 99%

Surface organization and composition of Euglena. II. Flagellar mastigonemes

Gb¹,

Rogalski²,

Valaitis³

1978

The Journal of Cell Biology

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The surface of the Euglena flagellum is coated with about 30,000 fine filaments of two distinct types. The longer of these nontubular mastigonemes (about 3 micron) appear to be attached to the paraflagellar rod whereas the shorter nontubular mastigonemes (about 1.5 micron) are the centrifugally arranged portions of a larger complex, which consists of an attached unit parallel to and outside of the flagellar membrane. Units are arranged laternally in near registration and longitudinally overlap by one-half of a unit length. Rows of mastigoneme units are firmly attached to the axoneme microtubules or to the paraflagellar rod as evidenced by their persistence after removal of the flagellar membrane with neutral detergents. SDS-acrylamide gels of whole flagella revealed about 30 polypeptides, of which two gave strong positive staining with the periodic acid-Schiff (PAS) procedure. At least one of these two bands (glycoproteins) has been equated with the surface mastigonemes by parallel analysis of isolated and purified mastigonemes, particularly after phenol extraction. The faster moving glycoprotein has been selectively removed from whole flagella and from the mastigoneme fraction with low concentrations of neutral detergents at neutral or high pH. The larger glycoprotein was found to be polydisperse when electrophoresed through 1% agarose/SDS gels. Thin-layer chromatography of hydrolysates of whole flagella or of isolated mastigonemes has indicated that the major carbohydrate moiety is the pentose sugar, xylose, with possibly a small amount of glucose and an unknown minor component.

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“…The location of the dense bands suggests a supportive role for them in the gametocyte pellicular complex. Although structures identical to the dense bands have not been reported previously, similar dense amorphous materials in Ochrornonas and Euglena connect axonemal microtubules to mastigonemes (flagellar hairs) or flagellar membranes [3, 71. After detergent treatment, which normally causes microtubules to separate from one another, they remained bound together by the dense extramicrotubular material [7]. If the dense material in P. falciparurn gametocytes serves a similar stabilizing function, it may connect not only the microtubules to each other, but also connect them collectively to the inner membrane.…”

Section: Results a N D Discussionmentioning

confidence: 99%