Editing Centrosome (section)

=== Structural aberrations ===
Usually, structural aberrations appear due to uncontrolled expression of centrosome components, or due to post-translational modifications (such as phosphorylations) that are not adequate for the components. These modifications may produce variations in centrosome size (usually too large, due to an excess of pericentriolar material). In addition, because centrosomal proteins have a tendency to form aggregates, centrosome-related bodies (CRBs) are often observed in ectopic places.<ref name=Casenghi2003>{{Cite journal
 | title = Polo-like kinase 1 regulates Nlp, a centrosome protein involved in microtubule nucleation
 | year = 2003
 | journal = Dev Cell
 | pages = 113–125
 | volume = 5
 | doi = 10.1016/S1534-5807(03)00193-X
 | last1 = Casenghi     | first1 =  M.
 | last2 =  Meraldi     | first2 =  P.
 | last3 =  Weinhart     | first3 =  U.
 | last4 =  Duncan     | first4 =  P.I.
 | last5 =  Korner     | first5 =  R.
 | last6 =  Nigg     | first6 =  E.A. | pmid=12852856
 | issue = 1
 | doi-access =  free
 }}</ref> Both enlarged centrosomes and CRBs are similar to the centrosomal structures observed in tumors.<ref name=Lingle2002>{{Cite journal
 | title = Centrosome amplification drives chromosomal instability in breast tumor development
 | year = 2002
 | journal = Proc Natl Acad Sci USA
 | pages = 1978–1983
 | volume = 99
 | pmid = 11830638
 | last1 = Lingle     | first1 =  W.L.
 | last2 =  Barrett     | first2 =  S.L.
 | last3 =  Negron     | first3 =  V.C.
 | last4 =  D'assoro     | first4 =  A.B.
 | last5 =  Boeneman     | first5 =  K.
 | last6 =  Liu  |first6= W.
 |last7= Whitehead |first7=C.M.
 | last8 =  Reynolds     | first8 =  C.
 | last9 =  Salisbury     | first9 =  J.L. | doi=10.1073/pnas.032479999 | pmc=122305
 | issue = 4
 | bibcode =2002PNAS...99.1978L| doi-access = free
 }}</ref> Even more, these structures can be induced in culture cells by overexpression of specific centrosomal proteins, such as CNap-1 or Nlp.<ref name=Casenghi2003 /><ref name=Fry1998>{{Cite journal
 | title = C-Nap1, a Novel Centrosomal Coiled-Coil Protein and Candidate Substrate of the Cell Cycle–regulated Protein Kinase Nek2
 | year = 1998
 | journal = J Cell Biol
 | pages = 1563–1574
 | volume = 141
 | last1 = Fry     | first1 =  A.M.
 | last2 =  Mayor     | first2 =  T.
 | last3 =  Meraldi     | first3 =  P.
 | last4 =  Stierhof     | first4 =  Y.D.
 | last5 =  Tanaka     | first5 =  K.
 | last6 =  Nigg     | first6 =  E.A.
 | issue=7
 | doi = 10.1083/jcb.141.7.1563
 | pmid = 9647649
 | pmc = 2133000
 }}</ref> These structures may look very similar, yet detailed studies reveal that they may present very different properties, depending on their proteic composition. For instance, their capacity to incorporate γ-TuRC complexes (see also: [[tubulin#γ-Tubulin|γ-tubulin]]) can be very variable, and so their capacity to nucleate [[microtubule]]s<ref name=Lingle2002 /> therefore affects the shape, polarity and motility of implicated tumor cells in different ways.