May 31, 2023 · Our atomic models provide insights into the conservation and specialization of axonemes, the interconnectivity between dyneins and their regulators, and the mechanisms that maintain axonemal...

In molecular biology, an axoneme, also called an axial filament, is the microtubule -based cytoskeletal structure that forms the core of a cilium or flagellum. [1][2] Cilia and flagella are found on many cells, organisms, and microorganisms, to provide motility.

Jan 2, 2023 · Our in situ data and processing strategies based on the contextual information revealed that the axoneme itself, which appeared to have ‘pseudo-ninefold symmetry’ in classical TEM images 3, is...

The core structure of the cilium, the axoneme, has a 9 + 2 microtubule (MT) architecture: two singlet MTs, known as the central pair (CP), and nine surrounding doublet MTs 4,5. The singlet MTs are hollow cylindrical structures formed by 13 protofilaments (PFs) of …

Historically, Transmission Electron Microscopy (TEM) was the mainstay of PCD diagnosis, surveying for disease-causing ultrastructural defects within individual ciliary axonemes. However, with advancement in PCD diagnostics, well-phenotyped cases of PCD, with normal or non-diagnostic ciliary ultrastructure, emerged frequently in diagnostic cohorts.

Aug 18, 2006 · Here we describe the three-dimensional structure of rapidly frozen axonemes from Chlamydomonas and sea urchin sperm, using cryoelectron tomography and image processing to focus on the motor enzyme dynein. Our images suggest a model for the way dynein generates force to slide microtubules.

May 5, 2020 · The existence of cytoplasmic factors required for PFR formation aligns with the concept that processes facilitating axoneme assembly occur across multiple compartments, and this is likely a common theme for extra-axonemal structure assembly.

We show a striking similarity between the microtubule axoneme structure of the Leishmania mexicana parasite infecting a macrophage and vertebrate primary cilia.

Jan 1, 2025 · We discover a sperm-specific, axoneme-tethered T-complex protein ring complex (TRiC) chaperone that may contribute to construction or maintenance of the long flagella of mammalian sperm.

Here we capitalize on recent developments in artificial intelligence-enabled structure prediction and cryo-electron microscopy (cryo-EM) to determine the structure of the 96-nm modular repeats of axonemes from the flagella of the alga Chlamydomonas reinhardtii and human respiratory cilia.