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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Light plays a significant role in regulating the growth and development of plants. In addition to providing energy for photosynthesis, light provides other important cues to regulate a range of developmental and physiological responses in plants.
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Positive regulators allow a cell to advance through cell cycle checkpoints. Negative regulators have an equally important role as they terminate a cell’s progression through the cell cycle—or pause it—until the cell meets specific criteria.
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To consistently produce healthy cells, the cell cycle—the process that generates daughter cells—must be precisely regulated.
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Related Experiment Video

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Large-Scale Purification of Porcine or Bovine Photoreceptor Outer Segments for Phagocytosis Assays on Retinal Pigment Epithelial Cells
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Kif17 phosphorylation regulates photoreceptor outer segment turnover.

Tylor R Lewis1, Sean R Kundinger2, Brian A Link1

  • 1Department of Cell Biology, Neurobiology, and Anatomy Medical College of Wisconsin, Milwaukee, WI, USA.

BMC Cell Biology
|November 22, 2018
PubMed
Summary
This summary is machine-generated.

Phosphorylation of KIF17 enhances its localization in photoreceptor outer segments, promoting disc shedding for cell maintenance. This finding reveals a novel role for KIF17 in photoreceptor homeostasis.

Keywords:
CiliaDisc sheddingIntraflagellar transportKinesinPhagocytosisPhotoreceptorRetina

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Area of Science:

  • Cell Biology
  • Ophthalmology
  • Molecular Motor Function

Background:

  • Kinesin family member 17 (KIF17) is a motor protein involved in intraflagellar transport and photoreceptor outer segment development.
  • The precise function of KIF17 in mature photoreceptors and the impact of its ciliary localization regulation remain incompletely understood.
  • Calcium/calmodulin-dependent protein kinase II (CaMKII) phosphorylation sites near KIF17's C-terminal consensus sequence suggest a potential regulatory mechanism for its localization and function.

Purpose of the Study:

  • To investigate the role of KIF17 phosphorylation in regulating its localization and function within mature photoreceptors.
  • To determine if CaMKII-mediated phosphorylation of KIF17 influences photoreceptor outer segment disc shedding and maintenance.

Main Methods:

  • Transgenic expression of wild-type and phospho-mimetic KIF17 in zebrafish photoreceptors.
  • Analysis of KIF17 localization and photoreceptor outer segment morphology in transgenic zebrafish and mouse models.
  • Assessment of disc shedding and photoreceptor outer segment turnover rates.

Main Results:

  • Phospho-mimetic KIF17 exhibited enhanced localization along the cone outer segment in zebrafish.
  • Expression of phospho-mimetic KIF17 led to increased photoreceptor outer segment disc shedding in a cell-autonomous manner.
  • Genetic mutations in KIF17 in zebrafish and mice resulted in diminished disc shedding, and CaMKII activation increased disc shedding in a KIF17-dependent manner.

Conclusions:

  • Phosphorylation of KIF17 is a key regulator of its photoreceptor outer segment localization and promotes disc shedding, a critical process for photoreceptor maintenance and homeostasis.
  • This study highlights the involvement of photoreceptor-derived signaling in the mechanisms of disc shedding, complementing existing research focused on retinal pigment epithelium phagocytosis.